IPNA_EMENI
ID IPNA_EMENI Reviewed; 331 AA.
AC P05326; C8VHS7; Q5BA08;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Isopenicillin N synthase {ECO:0000303|PubMed:3319778};
DE Short=IPNS {ECO:0000303|PubMed:3319778};
DE EC=1.21.3.1 {ECO:0000269|PubMed:3319778};
GN Name=ipnA {ECO:0000303|PubMed:3319778}; Synonyms=ips; ORFNames=AN2622;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=3319778; DOI=10.1016/0378-1119(87)90120-x;
RA Ramon D., Carramolino L., Patino C., Sanchez F., Penalva M.A.;
RT "Cloning and characterization of the isopenicillin N synthetase gene
RT mediating the formation of the beta-lactam ring in Aspergillus nidulans.";
RL Gene 57:171-181(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3045077; DOI=10.1128/jb.170.9.3817-3826.1988;
RA Weigel B.J., Burgett S.G., Chen V.J., Skatrud P.L., Frolik C.A.,
RA Queener S.W., Ingolia T.D.;
RT "Cloning and expression in Escherichia coli of isopenicillin N synthetase
RT genes from Streptomyces lipmanii and Aspergillus nidulans.";
RL J. Bacteriol. 170:3817-3826(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=7663335; DOI=10.1002/pro.5560040521;
RA Roach P.L., Schofield C.J., Baldwin J.E., Clifton I.J., Hajdu J.;
RT "Crystallization and preliminary X-ray diffraction studies on recombinant
RT isopenicillin N synthase from Aspergillus nidulans.";
RL Protein Sci. 4:1007-1009(1995).
RN [6] {ECO:0007744|PDB:1IPS}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR.
RX PubMed=7791906; DOI=10.1038/375700a0;
RA Roach P.L., Clifton I.J., Fueloep V., Harlos K., Barton G.J., Hajdu J.,
RA Andersson I., Schofield C.J., Baldwin J.E.;
RT "Crystal structure of isopenicillin N synthase is the first from a new
RT structural family of enzymes.";
RL Nature 375:700-704(1995).
RN [7] {ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON AND
RP N-[(5S)-5-AMINO-5-CARBOXYPENTANOYL]-L-CYSTEINYL-D-VALINE, AND COFACTOR.
RX PubMed=9194566; DOI=10.1038/42990;
RA Roach P.L., Clifton I.J., Hensgens C.M., Shibata N., Schofield C.J.,
RA Hajdu J., Baldwin J.E.;
RT "Structure of isopenicillin N synthase complexed with substrate and the
RT mechanism of penicillin formation.";
RL Nature 387:827-830(1997).
RN [8] {ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:1QJF}
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON;
RP N-[(5S)-5-AMINO-5-CARBOXYPENTANOYL]-L-CYSTEINYL-D-VALINE AND ISOPENICILLIN
RP N, AND COFACTOR.
RX PubMed=10537113; DOI=10.1038/44400;
RA Burzlaff N.I., Rutledge P.J., Clifton I.J., Hensgens C.M.H., Pickford M.,
RA Adlington R.M., Roach P.L., Baldwin J.E.;
RT "The reaction cycle of isopenicillin N synthase observed by X-ray
RT diffraction.";
RL Nature 401:721-724(1999).
RN [9] {ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4}
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11755401; DOI=10.1016/s1074-5521(01)00090-4;
RA Ogle J.M., Clifton I.J., Rutledge P.J., Elkins J.M., Burzlaff N.I.,
RA Adlington R.M., Roach P.L., Baldwin J.E.;
RT "Alternative oxidation by isopenicillin N synthase observed by X-ray
RT diffraction.";
RL Chem. Biol. 8:1231-1237(2001).
RN [10] {ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN}
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=12926272; DOI=10.1039/b212270g;
RA Elkins J.M., Rutledge P.J., Burzlaff N.I., Clifton I.J., Adlington R.M.,
RA Roach P.L., Baldwin J.E.;
RT "Crystallographic studies on the reaction of isopenicillin N synthase with
RT an unsaturated substrate analogue.";
RL Org. Biomol. Chem. 1:1455-1460(2003).
RN [11] {ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=12622704; DOI=10.1042/bj20021627;
RA Long A.J., Clifton I.J., Roach P.L., Baldwin J.E., Schofield C.J.,
RA Rutledge P.J.;
RT "Structural studies on the reaction of isopenicillin N synthase with the
RT substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-
RT aminobutyrate.";
RL Biochem. J. 372:687-693(2003).
RN [12] {ECO:0007744|PDB:1UZW}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=15175003; DOI=10.1042/bj20040529;
RA Grummitt A.R., Rutledge P.J., Clifton I.J., Baldwin J.E.;
RT "Active-site-mediated elimination of hydrogen fluoride from a fluorinated
RT substrate analogue by isopenicillin N synthase.";
RL Biochem. J. 382:659-666(2004).
RN [13] {ECO:0007744|PDB:2BU9}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=16143309; DOI=10.1016/j.bbrc.2005.08.155;
RA Howard-Jones A.R., Rutledge P.J., Clifton I.J., Adlington R.M.,
RA Baldwin J.E.;
RT "Unique binding of a non-natural L,L,L-substrate by isopenicillin N
RT synthase.";
RL Biochem. Biophys. Res. Commun. 336:702-708(2005).
RN [14] {ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=15850395; DOI=10.1021/bi047478q;
RA Long A.J., Clifton I.J., Roach P.L., Baldwin J.E., Rutledge P.J.,
RA Schofield C.J.;
RT "Structural studies on the reaction of isopenicillin N synthase with the
RT truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-
RT glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine.";
RL Biochemistry 44:6619-6628(2005).
RN [15] {ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=16444759; DOI=10.1002/cbic.200500282;
RA Daruzzaman A., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "Unexpected oxidation of a depsipeptide substrate analogue in crystalline
RT isopenicillin N synthase.";
RL ChemBioChem 7:351-358(2006).
RN [16] {ECO:0007744|PDB:2IVI, ECO:0007744|PDB:2IVJ}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=17397141; DOI=10.1021/bi062314q;
RA Howard-Jones A.R., Elkins J.M., Clifton I.J., Roach P.L., Adlington R.M.,
RA Baldwin J.E., Rutledge P.J.;
RT "Interactions of isopenicillin N synthase with cyclopropyl-containing
RT substrate analogues reveal new mechanistic insight.";
RL Biochemistry 46:4755-4762(2007).
RN [17] {ECO:0007744|PDB:2JB4}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=17907118; DOI=10.1002/cbic.200700176;
RA Stewart A.C., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "A cyclobutanone analogue mimics penicillin in binding to isopenicillin N
RT synthase.";
RL ChemBioChem 8:2003-2007(2007).
RN [18] {ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=18620394; DOI=10.1021/ja8005397;
RA Ge W., Clifton I.J., Stok J.E., Adlington R.M., Baldwin J.E.,
RA Rutledge P.J.;
RT "Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a
RT depsipeptide substrate analogue: implications for oxygen binding and a link
RT to nitrile hydratase?";
RL J. Am. Chem. Soc. 130:10096-10102(2008).
RN [19] {ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=19598184; DOI=10.1002/cbic.200900080;
RA Ge W., Clifton I.J., Howard-Jones A.R., Stok J.E., Adlington R.M.,
RA Baldwin J.E., Rutledge P.J.;
RT "Structural studies on the reaction of isopenicillin N synthase with a
RT sterically demanding depsipeptide substrate analogue.";
RL ChemBioChem 10:2025-2031(2009).
RN [20] {ECO:0007744|PDB:2VBP, ECO:0007744|PDB:2WO7}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=20603104; DOI=10.1016/j.bbrc.2010.06.129;
RA Ge W., Clifton I.J., Stok J.E., Adlington R.M., Baldwin J.E.,
RA Rutledge P.J.;
RT "Crystallographic studies on the binding of selectively deuterated LLD- and
RT LLL-substrate epimers by isopenicillin N synthase.";
RL Biochem. Biophys. Res. Commun. 398:659-664(2010).
RN [21] {ECO:0007744|PDB:2VBD}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=20024142; DOI=10.1039/b910170e;
RA Ge W., Clifton I.J., Stok J.E., Adlington R.M., Baldwin J.E.,
RA Rutledge P.J.;
RT "The crystal structure of an LLL-configured depsipeptide substrate analogue
RT bound to isopenicillin N synthase.";
RL Org. Biomol. Chem. 8:122-127(2010).
RN [22] {ECO:0007744|PDB:2Y60}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=22001738; DOI=10.1016/j.abb.2011.09.014;
RA Clifton I.J., Ge W., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "The crystal structure of isopenicillin N synthase with delta-((L)-alpha-
RT aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination
RT to iron.";
RL Arch. Biochem. Biophys. 516:103-107(2011).
RN [23] {ECO:0007744|PDB:2Y6F}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=21678539; DOI=10.1002/cbic.201100149;
RA Clifton I.J., Ge W., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "Isopenicillin N synthase binds delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-
RT thia-allo-isoleucine through both sulfur atoms.";
RL ChemBioChem 12:1881-1885(2011).
RN [24] {ECO:0007744|PDB:4BB3}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=23262315; DOI=10.1016/j.abb.2012.12.012;
RA Daruzzaman A., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "The crystal structure of isopenicillin N synthase with a dipeptide
RT substrate analogue.";
RL Arch. Biochem. Biophys. 530:48-53(2013).
RN [25] {ECO:0007744|PDB:3ZKU, ECO:0007744|PDB:3ZKY}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOGS.
RX PubMed=23468426; DOI=10.1002/cbic.201200728;
RA Daruzzaman A., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "The interaction of isopenicillin N synthase with homologated substrate
RT analogues delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-Xaa characterised
RT by protein crystallography.";
RL ChemBioChem 14:599-606(2013).
RN [26] {ECO:0007744|PDB:3ZOI}
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=23860486; DOI=10.1016/j.febslet.2013.07.016;
RA Clifton I.J., Ge W., Adlington R.M., Baldwin J.E., Rutledge P.J.;
RT "The crystal structure of an isopenicillin N synthase complex with an
RT ethereal substrate analogue reveals water in the oxygen binding site.";
RL FEBS Lett. 587:2705-2709(2013).
RN [27] {ECO:0007744|PDB:2BJS}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1-325 IN COMPLEX WITH IRON AND
RP N-[(5S)-5-AMINO-5-CARBOXYPENTANOYL]-L-CYSTEINYL-D-VALINE, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-98; LEU-223; LEU-231; VAL-272
RP AND PRO-283.
RX PubMed=28703303; DOI=10.1002/chem.201701592;
RA McNeill L.A., Brown T.J.N., Sami M., Clifton I.J., Burzlaff N.I.,
RA Claridge T.D.W., Adlington R.M., Baldwin J.E., Rutledge P.J.,
RA Schofield C.J.;
RT "Terminally truncated isopenicillin N synthase generates a dithioester
RT product: evidence for a thioaldehyde intermediate during catalysis and a
RT new mode of reaction for non-Heme iron oxidases.";
RL Chemistry 23:12815-12824(2017).
RN [28] {ECO:0007744|PDB:6Y0O}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX PubMed=32939282; DOI=10.1107/s2052252520010374;
RA Rabe P., Beale J.H., Butryn A., Aller P., Dirr A., Lang P.A., Axford D.N.,
RA Carr S.B., Leissing T.M., McDonough M.A., Davy B., Ebrahim A., Orlans J.,
RA Storm S.L.S., Orville A.M., Schofield C.J., Owen R.L.;
RT "Anaerobic fixed-target serial crystallography.";
RL IUCrJ 7:901-912(2020).
RN [29] {ECO:0007744|PDB:6ZAK}
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RA Rabe P., Kamps J.J.A.G., Sutherlin K., Pharm C., McDonough M.A.,
RA Leissing T.M., Aller P., Butryn A., Linyard J., Lang P., Brem J.,
RA Fuller F.D., Batyuk A., Hunter M.S., Pettinati I., Clifton I.J.,
RA Alonso-Mori R., Gul S., Young I., Kim I., Bhowmick A., O'Riordan L.,
RA Brewster A.S., Claridge T.D.W., Sauter N.K., Yachandra V., Yano J.,
RA Kern J.F., Orville A.M., Schofield C.J.;
RT "Room temperature XFEL isopenicillin N synthase structure in complex with
RT the Fe(IV)=O mimic VO and ACV.";
RL Submitted (JUN-2020) to the PDB data bank.
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE
RP ANALOG.
RX PubMed=34417180; DOI=10.1126/sciadv.abh0250;
RA Rabe P., Kamps J.J.A.G., Sutherlin K.D., Linyard J.D.S., Aller P.,
RA Pham C.C., Makita H., Clifton I., McDonough M.A., Leissing T.M., Shutin D.,
RA Lang P.A., Butryn A., Brem J., Gul S., Fuller F.D., Kim I.S., Cheah M.H.,
RA Fransson T., Bhowmick A., Young I.D., O'Riordan L., Brewster A.S.,
RA Pettinati I., Doyle M., Joti Y., Owada S., Tono K., Batyuk A., Hunter M.S.,
RA Alonso-Mori R., Bergmann U., Owen R.L., Sauter N.K., Claridge T.D.W.,
RA Robinson C.V., Yachandra V.K., Yano J., Kern J.F., Orville A.M.,
RA Schofield C.J.;
RT "X-ray free-electron laser studies reveal correlated motion during
RT isopenicillin N synthase catalysis.";
RL Sci. Adv. 7:0-0(2021).
CC -!- FUNCTION: Isopenicillin N synthase; part of the gene cluster that
CC mediates the biosynthesis of penicillin, the world's most important
CC antibiotic (PubMed:3319778, PubMed:11755401). IpnA catalyzes the
CC cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-
CC cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that
CC contains the beta-lactam nucleus (PubMed:3319778, PubMed:11755401,
CC PubMed:28703303). The penicillin biosynthesis occurs via 3 enzymatic
CC steps, the first corresponding to the production of the tripeptide N-
CC [(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV)
CC by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin
CC N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam
CC nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for
CC phenylacetic acid by the isopenicillin N acyltransferase penDE to yield
CC penicillin in the peroxisomal matrix (By similarity).
CC {ECO:0000250|UniProtKB:P08703, ECO:0000269|PubMed:11755401,
CC ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:3319778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
CC = 2 H2O + isopenicillin N; Xref=Rhea:RHEA:22428, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:58399, ChEBI:CHEBI:58572; EC=1.21.3.1;
CC Evidence={ECO:0000269|PubMed:11755401, ECO:0000269|PubMed:28703303,
CC ECO:0000269|PubMed:3319778};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22429;
CC Evidence={ECO:0000269|PubMed:11755401, ECO:0000269|PubMed:28703303,
CC ECO:0000269|PubMed:3319778};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:10537113, ECO:0000269|PubMed:7791906,
CC ECO:0000269|PubMed:9194566};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805, ECO:0000269|PubMed:10537113,
CC ECO:0000269|PubMed:7791906, ECO:0000269|PubMed:9194566};
CC -!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin
CC G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3.
CC {ECO:0000269|PubMed:3319778}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P05189}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P08703}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; M18111; AAA33311.1; -; Genomic_DNA.
DR EMBL; M21882; AAA33310.1; -; Genomic_DNA.
DR EMBL; AACD01000045; EAA62969.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF84347.1; -; Genomic_DNA.
DR PIR; A27355; A27355.
DR RefSeq; XP_660226.1; XM_655134.1.
DR PDB; 1BK0; X-ray; 1.30 A; A=1-331.
DR PDB; 1BLZ; X-ray; 1.45 A; A=1-331.
DR PDB; 1HB1; X-ray; 1.55 A; A=1-331.
DR PDB; 1HB2; X-ray; 1.30 A; A=1-331.
DR PDB; 1HB3; X-ray; 1.40 A; A=1-331.
DR PDB; 1HB4; X-ray; 1.50 A; A=1-331.
DR PDB; 1IPS; X-ray; 2.50 A; A/B=1-331.
DR PDB; 1OBN; X-ray; 1.30 A; A=1-331.
DR PDB; 1OC1; X-ray; 2.20 A; A=1-331.
DR PDB; 1ODM; X-ray; 1.15 A; A=1-331.
DR PDB; 1ODN; X-ray; 1.60 A; A=1-331.
DR PDB; 1QIQ; X-ray; 1.50 A; A=1-331.
DR PDB; 1QJE; X-ray; 1.35 A; A=1-331.
DR PDB; 1QJF; X-ray; 1.40 A; A=1-331.
DR PDB; 1UZW; X-ray; 1.30 A; A=1-331.
DR PDB; 1W03; X-ray; 2.10 A; A=1-331.
DR PDB; 1W04; X-ray; 1.28 A; A=1-331.
DR PDB; 1W05; X-ray; 2.46 A; A=1-331.
DR PDB; 1W06; X-ray; 1.65 A; A=1-331.
DR PDB; 1W3V; X-ray; 1.40 A; A=1-331.
DR PDB; 1W3X; X-ray; 1.46 A; A=1-331.
DR PDB; 2BJS; X-ray; 1.30 A; A=1-325.
DR PDB; 2BU9; X-ray; 1.30 A; A=1-331.
DR PDB; 2IVI; X-ray; 1.30 A; B=1-331.
DR PDB; 2IVJ; X-ray; 1.46 A; A=1-331.
DR PDB; 2JB4; X-ray; 1.30 A; A=1-331.
DR PDB; 2VAU; X-ray; 1.80 A; A=1-331.
DR PDB; 2VBB; X-ray; 1.40 A; A=1-331.
DR PDB; 2VBD; X-ray; 2.00 A; A=1-331.
DR PDB; 2VBP; X-ray; 1.50 A; A=1-331.
DR PDB; 2VCM; X-ray; 1.65 A; A=1-331.
DR PDB; 2VE1; X-ray; 2.20 A; A=1-331.
DR PDB; 2WO7; X-ray; 2.50 A; A=1-331.
DR PDB; 2Y60; X-ray; 1.40 A; A=1-331.
DR PDB; 2Y6F; X-ray; 1.79 A; A=1-331.
DR PDB; 3ZKU; X-ray; 1.40 A; A=1-331.
DR PDB; 3ZKY; X-ray; 1.45 A; A=1-331.
DR PDB; 3ZOI; X-ray; 1.82 A; A=1-331.
DR PDB; 4BB3; X-ray; 1.40 A; A=1-331.
DR PDB; 6Y0O; X-ray; 2.20 A; A=1-331.
DR PDB; 6Y0P; X-ray; 1.98 A; A=1-331.
DR PDB; 6ZAE; X-ray; 1.40 A; A=1-331.
DR PDB; 6ZAF; X-ray; 1.40 A; A=1-331.
DR PDB; 6ZAG; X-ray; 1.40 A; A=1-331.
DR PDB; 6ZAH; X-ray; 1.43 A; A=1-331.
DR PDB; 6ZAI; X-ray; 1.55 A; A=1-331.
DR PDB; 6ZAJ; X-ray; 1.53 A; A=1-331.
DR PDB; 6ZAK; X-ray; 1.54 A; A=1-331.
DR PDB; 6ZAL; X-ray; 1.83 A; A=1-331.
DR PDB; 6ZAM; X-ray; 1.55 A; A=1-331.
DR PDB; 6ZAN; X-ray; 1.35 A; A=1-331.
DR PDB; 6ZAO; X-ray; 1.66 A; A=1-331.
DR PDB; 6ZAP; X-ray; 1.36 A; A=1-331.
DR PDB; 6ZAQ; X-ray; 1.60 A; A=1-331.
DR PDB; 6ZW8; X-ray; 1.22 A; A=1-331.
DR PDBsum; 1BK0; -.
DR PDBsum; 1BLZ; -.
DR PDBsum; 1HB1; -.
DR PDBsum; 1HB2; -.
DR PDBsum; 1HB3; -.
DR PDBsum; 1HB4; -.
DR PDBsum; 1IPS; -.
DR PDBsum; 1OBN; -.
DR PDBsum; 1OC1; -.
DR PDBsum; 1ODM; -.
DR PDBsum; 1ODN; -.
DR PDBsum; 1QIQ; -.
DR PDBsum; 1QJE; -.
DR PDBsum; 1QJF; -.
DR PDBsum; 1UZW; -.
DR PDBsum; 1W03; -.
DR PDBsum; 1W04; -.
DR PDBsum; 1W05; -.
DR PDBsum; 1W06; -.
DR PDBsum; 1W3V; -.
DR PDBsum; 1W3X; -.
DR PDBsum; 2BJS; -.
DR PDBsum; 2BU9; -.
DR PDBsum; 2IVI; -.
DR PDBsum; 2IVJ; -.
DR PDBsum; 2JB4; -.
DR PDBsum; 2VAU; -.
DR PDBsum; 2VBB; -.
DR PDBsum; 2VBD; -.
DR PDBsum; 2VBP; -.
DR PDBsum; 2VCM; -.
DR PDBsum; 2VE1; -.
DR PDBsum; 2WO7; -.
DR PDBsum; 2Y60; -.
DR PDBsum; 2Y6F; -.
DR PDBsum; 3ZKU; -.
DR PDBsum; 3ZKY; -.
DR PDBsum; 3ZOI; -.
DR PDBsum; 4BB3; -.
DR PDBsum; 6Y0O; -.
DR PDBsum; 6Y0P; -.
DR PDBsum; 6ZAE; -.
DR PDBsum; 6ZAF; -.
DR PDBsum; 6ZAG; -.
DR PDBsum; 6ZAH; -.
DR PDBsum; 6ZAI; -.
DR PDBsum; 6ZAJ; -.
DR PDBsum; 6ZAK; -.
DR PDBsum; 6ZAL; -.
DR PDBsum; 6ZAM; -.
DR PDBsum; 6ZAN; -.
DR PDBsum; 6ZAO; -.
DR PDBsum; 6ZAP; -.
DR PDBsum; 6ZAQ; -.
DR PDBsum; 6ZW8; -.
DR AlphaFoldDB; P05326; -.
DR SMR; P05326; -.
DR STRING; 162425.CADANIAP00010504; -.
DR EnsemblFungi; CBF84347; CBF84347; ANIA_02622.
DR EnsemblFungi; EAA62969; EAA62969; AN2622.2.
DR GeneID; 2874542; -.
DR KEGG; ani:AN2622.2; -.
DR VEuPathDB; FungiDB:AN2622; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_6_1_1; -.
DR InParanoid; P05326; -.
DR OMA; EADDNAY; -.
DR OrthoDB; 755305at2759; -.
DR BRENDA; 1.21.3.1; 517.
DR UniPathway; UPA00149; UER00240.
DR EvolutionaryTrace; P05326; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; ISS:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016216; F:isopenicillin-N synthase activity; IDA:AspGD.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0042318; P:penicillin biosynthetic process; IDA:AspGD.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR002057; Isopenicillin-N_synth_CS.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS00185; IPNS_1; 1.
DR PROSITE; PS00186; IPNS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Cytoplasm; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Vitamin C.
FT CHAIN 1..331
FT /note="Isopenicillin N synthase"
FT /id="PRO_0000219498"
FT DOMAIN 176..288
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 87
FT /ligand="isopenicillin N"
FT /ligand_id="ChEBI:CHEBI:58399"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0007744|PDB:1QJE"
FT BINDING 87
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:2BJS"
FT BINDING 91
FT /ligand="isopenicillin N"
FT /ligand_id="ChEBI:CHEBI:58399"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0007744|PDB:1QJE"
FT BINDING 91
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:2BJS"
FT BINDING 183
FT /ligand="isopenicillin N"
FT /ligand_id="ChEBI:CHEBI:58399"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0007744|PDB:1QJE"
FT BINDING 183
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566,
FT ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS"
FT BINDING 189
FT /ligand="isopenicillin N"
FT /ligand_id="ChEBI:CHEBI:58399"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0007744|PDB:1QJE"
FT BINDING 189
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:2BJS"
FT BINDING 214
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ,
FT ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2,
FT ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4,
FT ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1,
FT ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN,
FT ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW,
FT ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04,
FT ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06,
FT ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X,
FT ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI,
FT ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4,
FT ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB,
FT ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP,
FT ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1,
FT ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60,
FT ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU,
FT ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3"
FT BINDING 214
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE"
FT BINDING 216
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ,
FT ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2,
FT ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4,
FT ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1,
FT ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN,
FT ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW,
FT ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04,
FT ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06,
FT ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X,
FT ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI,
FT ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4,
FT ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB,
FT ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP,
FT ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1,
FT ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60,
FT ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU,
FT ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3"
FT BINDING 216
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:2BJS"
FT BINDING 270
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ,
FT ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2,
FT ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4,
FT ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1,
FT ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN,
FT ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW,
FT ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04,
FT ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06,
FT ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X,
FT ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI,
FT ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4,
FT ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB,
FT ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP,
FT ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1,
FT ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60,
FT ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU,
FT ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3"
FT BINDING 279
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 281
FT /ligand="isopenicillin N"
FT /ligand_id="ChEBI:CHEBI:58399"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0007744|PDB:1QJE"
FT BINDING 281
FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-
FT valine"
FT /ligand_id="ChEBI:CHEBI:58572"
FT /evidence="ECO:0000269|PubMed:10537113,
FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566,
FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE,
FT ECO:0007744|PDB:2BJS"
FT SITE 211
FT /note="Transition state stabilizer"
FT /evidence="ECO:0007744|PDB:1QJE"
FT MUTAGEN 98
FT /note="K->E: Strongly reduced the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT MUTAGEN 223
FT /note="L->I,V: Strongly reduced the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT MUTAGEN 231
FT /note="L->I,V: Strongly reduced the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT MUTAGEN 231
FT /note="L->T: Abolishes the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT MUTAGEN 272
FT /note="V->T: Strongly reduced the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT MUTAGEN 283
FT /note="P->A,I,V: Strongly reduced the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT MUTAGEN 283
FT /note="P->L: Abolishes the catalytic activity."
FT /evidence="ECO:0000269|PubMed:28703303"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:1ODM"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1ODM"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1ODM"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 138..163
FT /evidence="ECO:0007829|PDB:1ODM"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1ODM"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1ODM"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:1ODM"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:1ODM"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6ZAQ"
FT HELIX 313..328
FT /evidence="ECO:0007829|PDB:1ODM"
SQ SEQUENCE 331 AA; 37522 MW; 5BA1A726E9EEFA25 CRC64;
MGSVSKANVP KIDVSPLFGD DQAAKMRVAQ QIDAASRDTG FFYAVNHGIN VQRLSQKTKE
FHMSITPEEK WDLAIRAYNK EHQDQVRAGY YLSIPGKKAV ESFCYLNPNF TPDHPRIQAK
TPTHEVNVWP DETKHPGFQD FAEQYYWDVF GLSSALLKGY ALALGKEENF FARHFKPDDT
LASVVLIRYP YLDPYPEAAI KTAADGTKLS FEWHEDVSLI TVLYQSNVQN LQVETAAGYQ
DIEADDTGYL INCGSYMAHL TNNYYKAPIH RVKWVNAERQ SLPFFVNLGY DSVIDPFDPR
EPNGKSDREP LSYGDYLQNG LVSLINKNGQ T
