SIDA_ASPFU
ID SIDA_ASPFU Reviewed; 501 AA.
AC E9QYP0; Q4X250; Q5SE95;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:15504822};
DE Short=OMO {ECO:0000250|UniProtKB:G5EB76};
DE EC=1.14.13.196 {ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:16113265};
DE AltName: Full=Siderophore biosynthesis protein A {ECO:0000303|PubMed:15504822};
GN Name=sidA {ECO:0000303|PubMed:15504822}; ORFNames=Afu2g07680;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15504822; DOI=10.1084/jem.20041242;
RA Schrettl M., Bignell E., Kragl C., Joechl C., Rogers T., Arst H.N. Jr.,
RA Haynes K., Haas H.;
RT "Siderophore biosynthesis but not reductive iron assimilation is essential
RT for Aspergillus fumigatus virulence.";
RL J. Exp. Med. 200:1213-1219(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NIH 5233 / ATCC 13073;
RX PubMed=16113265; DOI=10.1128/iai.73.9.5493-5503.2005;
RA Hissen A.H., Wan A.N., Warwas M.L., Pinto L.J., Moore M.M.;
RT "The Aspergillus fumigatus siderophore biosynthetic gene sidA, encoding L-
RT ornithine N(5)-oxygenase, is required for virulence.";
RL Infect. Immun. 73:5493-5503(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17845073; DOI=10.1371/journal.ppat.0030128;
RA Schrettl M., Bignell E., Kragl C., Sabiha Y., Loss O., Eisendle M.,
RA Wallner A., Arst H.N. Jr., Haynes K., Haas H.;
RT "Distinct roles for intra- and extracellular siderophores during
RT Aspergillus fumigatus infection.";
RL PLoS Pathog. 3:1195-1207(2007).
RN [5]
RP INDUCTION.
RX PubMed=18721228; DOI=10.1111/j.1365-2958.2008.06376.x;
RA Schrettl M., Kim H.S., Eisendle M., Kragl C., Nierman W.C., Heinekamp T.,
RA Werner E.R., Jacobsen I., Illmer P., Yi H., Brakhage A.A., Haas H.;
RT "SreA-mediated iron regulation in Aspergillus fumigatus.";
RL Mol. Microbiol. 70:27-43(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP PATHWAY, SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=20614882; DOI=10.1021/bi100291n;
RA Chocklett S.W., Sobrado P.;
RT "Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with
RT bound flavin cofactor.";
RL Biochemistry 49:6777-6783(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=20650894; DOI=10.1074/jbc.m110.157578;
RA Mayfield J.A., Frederick R.E., Streit B.R., Wencewicz T.A., Ballou D.P.,
RA DuBois J.L.;
RT "Comprehensive spectroscopic, steady state, and transient kinetic studies
RT of a representative siderophore-associated flavin monooxygenase.";
RL J. Biol. Chem. 285:30375-30388(2010).
RN [8]
RP FUNCTION.
RX PubMed=21622789; DOI=10.1128/aem.00182-11;
RA Blatzer M., Schrettl M., Sarg B., Lindner H.H., Pfaller K., Haas H.;
RT "SidL, an Aspergillus fumigatus transacetylase involved in biosynthesis of
RT the siderophores ferricrocin and hydroxyferricrocin.";
RL Appl. Environ. Microbiol. 77:4959-4966(2011).
RN [9]
RP FUNCTION.
RX PubMed=22465572; DOI=10.1016/j.bbapap.2012.03.004;
RA Romero E., Fedkenheuer M., Chocklett S.W., Qi J., Oppenheimer M.,
RA Sobrado P.;
RT "Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating
RT monooxygenase.";
RL Biochim. Biophys. Acta 1824:850-857(2012).
RN [10]
RP FUNCTION.
RX PubMed=22106303; DOI=10.1073/pnas.1106399108;
RA Yasmin S., Alcazar-Fuoli L., Gruendlinger M., Puempel T., Cairns T.,
RA Blatzer M., Lopez J.F., Grimalt J.O., Bignell E., Haas H.;
RT "Mevalonate governs interdependency of ergosterol and siderophore
RT biosyntheses in the fungal pathogen Aspergillus fumigatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E497-E504(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD; NADP;
RP L-ORNITHINE; LYSINE AND L-ARGININE.
RX PubMed=22928747; DOI=10.1021/bi301072w;
RA Franceschini S., Fedkenheuer M., Vogelaar N.J., Robinson H.H., Sobrado P.,
RA Mattevi A.;
RT "Structural insight into the mechanism of oxygen activation and substrate
RT selectivity of flavin-dependent N-hydroxylating monooxygenases.";
RL Biochemistry 51:7043-7045(2012).
CC -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore
CC biosynthetic pathway (PubMed:15504822, PubMed:16113265,
CC PubMed:17845073, PubMed:20614882, PubMed:20650894, PubMed:22465572).
CC Aspergillus fumigatus produces four types of siderophores, low-
CC molecular-mass iron chelators, including excreted fusarinine C (FsC)
CC and triacetylfusarinine C (TAFC) for iron uptake; and intacellular
CC ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial
CC iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-
CC anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by
CC ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-
CC (N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four
CC siderophores depends on the hydroxylation of ornithine, catalyzed by
CC the monooxygenase sidA (PubMed:15504822, PubMed:16113265,
CC PubMed:20614882, PubMed:20650894, PubMed:22465572). SidA is highly
CC specific for its substrate, only hydrolyzing l-ornithine, and has
CC preference for NADPH over NADH, NADPH playing a role in stabilization
CC of the C4a-hydroperoxyflavin intermediate (PubMed:20614882,
CC PubMed:22465572). Subsequently, the pathways for biosynthesis of
CC extra- and intracellular siderophores split (PubMed:17845073). For
CC biosynthesis of extracellular siderophores, the transacylase sidF
CC transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073).
CC The required anhydromevalonyl-CoA moiety is derived from mevalonate by
CC CoA ligation and dehydration catalyzed by sidI and sidH respectively
CC (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC
CC biosynthesis involves the constitutively expressed sidL
CC (PubMed:21622789). FC is hydroxylated to HFC by an as yet
CC uncharacterized enzyme during conidiation (PubMed:17845073). Assembly
CC of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal
CC peptide synthetases (NRPS), sidD and sidC respectively
CC (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC
CC for forming TAFC (PubMed:17845073). Both extra- and intracellular
CC siderophores are crucial for growth during iron limitation and
CC virulence (PubMed:16113265). {ECO:0000269|PubMed:15504822,
CC ECO:0000269|PubMed:16113265, ECO:0000269|PubMed:17845073,
CC ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894,
CC ECO:0000269|PubMed:21622789, ECO:0000269|PubMed:22106303,
CC ECO:0000269|PubMed:22465572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78275; EC=1.14.13.196;
CC Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC NAD(+); Xref=Rhea:RHEA:41512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78275; EC=1.14.13.196;
CC Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894,
CC ECO:0000269|PubMed:22928747};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:20614882,
CC ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22928747};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for L-ornithine (in the presence of 1 mM NADH)
CC {ECO:0000269|PubMed:20614882};
CC KM=1.7 mM for L-ornithine (in the presence of 1 mM NADPH)
CC {ECO:0000269|PubMed:20614882};
CC KM=0.49 mM for L-ornithine (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20650894};
CC KM=0.58 mM for L-ornithine (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:20650894};
CC KM=0.94 mM for NADPH (in the presence of 15 mM L-ornithine)
CC {ECO:0000269|PubMed:20614882};
CC KM=0.90 mM for NADH (in the presence of 15 mM L-ornithine)
CC {ECO:0000269|PubMed:20614882};
CC KM=4.6 uM for NADPH (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20650894};
CC KM=2.6 uM for NADPH (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:20650894};
CC KM=18 uM for O(2) (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:20650894};
CC KM=16 uM for O(2) (at 25 degrees Celsius)
CC {ECO:0000269|PubMed:20650894};
CC Note=kcat is 29 min(-1) with L-ornithine as substrate and 75 min(-1)
CC with NADPH as substrate. {ECO:0000269|PubMed:20614882};
CC -!- PATHWAY: Siderophore biosynthesis; ferrichrome biosynthesis.
CC {ECO:0000269|PubMed:15504822, ECO:0000269|PubMed:16113265,
CC ECO:0000269|PubMed:17845073, ECO:0000269|PubMed:20614882,
CC ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22465572}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20614882}.
CC -!- MASS SPECTROMETRY: Mass=57210; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20614882};
CC -!- DISRUPTION PHENOTYPE: Moderatley reduced growth rate during iron
CC starvation and in iron replete conditions. Only displays 1% of wild-
CC type conidiospore production in iron-depleted and replete conditions.
CC Completely attenuates virulence in a mouse model of invasive pulmonary
CC aspergillosis. {ECO:0000269|PubMed:15504822,
CC ECO:0000269|PubMed:16113265}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; AY586511; AAT84594.1; -; Genomic_DNA.
DR EMBL; AY819708; AAX40989.1; -; Genomic_DNA.
DR EMBL; AAHF01000001; EAL93065.1; -; Genomic_DNA.
DR RefSeq; XP_755103.1; XM_750010.1.
DR PDB; 4B63; X-ray; 1.90 A; A=1-501.
DR PDB; 4B64; X-ray; 2.28 A; A=1-501.
DR PDB; 4B65; X-ray; 2.32 A; A=1-501.
DR PDB; 4B66; X-ray; 2.90 A; A=1-501.
DR PDB; 4B67; X-ray; 2.75 A; A=1-501.
DR PDB; 4B68; X-ray; 2.29 A; A=1-501.
DR PDB; 4B69; X-ray; 2.30 A; A=1-501.
DR PDB; 4NZH; X-ray; 2.00 A; A=1-501.
DR PDB; 5CKU; X-ray; 2.10 A; A=1-501.
DR PDB; 6X0H; X-ray; 2.09 A; A/B/C/D=29-501.
DR PDB; 6X0I; X-ray; 1.95 A; A/B/C/D=1-501.
DR PDB; 6X0J; X-ray; 2.33 A; A/B/C/D=29-501.
DR PDB; 6X0K; X-ray; 2.23 A; A/B/C/D/E/F/G/H=29-501.
DR PDB; 7JVK; X-ray; 2.20 A; A/B/C/D=1-501.
DR PDB; 7JVL; X-ray; 2.10 A; A/B/C/D=1-501.
DR PDBsum; 4B63; -.
DR PDBsum; 4B64; -.
DR PDBsum; 4B65; -.
DR PDBsum; 4B66; -.
DR PDBsum; 4B67; -.
DR PDBsum; 4B68; -.
DR PDBsum; 4B69; -.
DR PDBsum; 4NZH; -.
DR PDBsum; 5CKU; -.
DR PDBsum; 6X0H; -.
DR PDBsum; 6X0I; -.
DR PDBsum; 6X0J; -.
DR PDBsum; 6X0K; -.
DR PDBsum; 7JVK; -.
DR PDBsum; 7JVL; -.
DR AlphaFoldDB; E9QYP0; -.
DR SMR; E9QYP0; -.
DR STRING; 746128.CADAFUBP00002315; -.
DR ChEMBL; CHEMBL4295542; -.
DR EnsemblFungi; EAL93065; EAL93065; AFUA_2G07680.
DR GeneID; 3513640; -.
DR KEGG; afm:AFUA_2G07680; -.
DR VEuPathDB; FungiDB:Afu2g07680; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_020931_2_0_1; -.
DR InParanoid; E9QYP0; -.
DR OMA; YHGNTNY; -.
DR OrthoDB; 1235295at2759; -.
DR BRENDA; 1.14.13.195; 508.
DR BRENDA; 1.14.13.196; 508.
DR UniPathway; UPA00783; -.
DR PHI-base; PHI:377; -.
DR PHI-base; PHI:486; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005506; F:iron ion binding; IDA:AspGD.
DR GO; GO:0004497; F:monooxygenase activity; IDA:AspGD.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IDA:AspGD.
DR GO; GO:0070401; F:NADP+ binding; IDA:AspGD.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:AspGD.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:AspGD.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:AspGD.
DR GO; GO:0031169; P:ferrichrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR GO; GO:0019290; P:siderophore biosynthetic process; IMP:AspGD.
DR GO; GO:0033214; P:siderophore-dependent iron import into cell; IMP:AspGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR42802; PTHR42802; 1.
DR Pfam; PF13434; K_oxygenase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Monooxygenase; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..501
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000431070"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 254..257
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 293..296
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 323..325
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 466..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22928747"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22928747"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:4B63"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6X0H"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4B63"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 162..174
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:4B63"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4B67"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4B63"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:4NZH"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 359..366
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 374..381
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 417..422
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:4B63"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:4B63"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:4B63"
FT TURN 463..466
FT /evidence="ECO:0007829|PDB:4B63"
FT HELIX 471..490
FT /evidence="ECO:0007829|PDB:4B63"
SQ SEQUENCE 501 AA; 56877 MW; DD1D4DEDD2509506 CRC64;
MESVERKSES SYLGMRNMQP EQRLSLDPPR LRSTPQDELH DLLCVGFGPA SLAIAIALHD
ALDPRLNKSA SNIHAQPKIC FLERQKQFAW HSGMLVPGSK MQISFIKDLA TLRDPRSSFT
FLNYLHQKGR LIHFTNLSTF LPARLEFEDY MRWCAQQFSD VVAYGEEVVE VIPGKSDPSS
SVVDFFTVRS RNVETGEISA RRTRKVVIAI GGTAKMPSGL PQDPRIIHSS KYCTTLPALL
KDKSKPYNIA VLGSGQSAAE IFHDLQKRYP NSRTTLIMRD SAMRPSDDSP FVNEIFNPER
VDKFYSQSAA ERQRSLLADK ATNYSVVRLE LIEEIYNDMY LQRVKNPDET QWQHRILPER
KITRVEHHGP QSRMRIHLKS SKPESEGAAN DVKETLEVDA LMVATGYNRN AHERLLSKVQ
HLRPTGQDQW KPHRDYRVEM DPSKVSSEAG IWLQGCNERT HGLSDSLLSV LAVRGGEMVQ
SIFGEQLERA AVQGHQLRAM L
