HIS5B_ARATH
ID HIS5B_ARATH Reviewed; 272 AA.
AC O23346; Q94AE6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase 2, chloroplastic {ECO:0000303|PubMed:16547652};
DE Short=IGPD 2 {ECO:0000303|PubMed:16547652};
DE EC=4.2.1.19 {ECO:0000269|PubMed:26095028};
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 5B {ECO:0000303|PubMed:16547652};
DE Flags: Precursor;
GN Name=HISN5B {ECO:0000303|PubMed:16547652};
GN OrderedLocusNames=At4g14910 {ECO:0000312|Araport:AT4G14910};
GN ORFNames=dl3495c {ECO:0000312|EMBL:CAB10270.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547652; DOI=10.1007/s00726-005-0247-0;
RA Stepansky A., Leustek T.;
RT "Histidine biosynthesis in plants.";
RL Amino Acids 30:127-142(2006).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17434988; DOI=10.1104/pp.107.096511;
RA Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.;
RT "Genetic dissection of histidine biosynthesis in Arabidopsis.";
RL Plant Physiol. 144:890-903(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 69-272 IN COMPLEX WITH MANGANESE
RP AND SUBSTRATE, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, ACTIVITY REGULATION,
RP AND MUTAGENESIS OF GLU-73.
RX PubMed=26095028; DOI=10.1016/j.str.2015.05.012;
RA Bisson C., Britton K.L., Sedelnikova S.E., Rodgers H.F., Eadsforth T.C.,
RA Viner R.C., Hawkes T.R., Baker P.J., Rice D.W.;
RT "Crystal structures reveal that the reaction mechanism of
RT imidazoleglycerol-phosphate dehydratase is controlled by switching Mn(II)
RT coordination.";
RL Structure 23:1236-1245(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 69-272 IN COMPLEX WITH C348;
RP MANGANESE AND SUBSTRATE, AND ACTIVITY REGULATION.
RX PubMed=27717128; DOI=10.1002/anie.201607185;
RA Bisson C., Britton K.L., Sedelnikova S.E., Rodgers H.F., Eadsforth T.C.,
RA Viner R.C., Hawkes T.R., Baker P.J., Rice D.W.;
RT "Mirror-image packing provides a molecular basis for the nanomolar
RT equipotency of enantiomers of an experimental herbicide.";
RL Angew. Chem. Int. Ed. Engl. 55:13485-13489(2016).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 69-272 IN COMPLEX WITH
RP C348.
RX PubMed=29434040; DOI=10.1073/pnas.1708839115;
RA Rawson S., Bisson C., Hurdiss D.L., Fazal A., McPhillie M.J.,
RA Sedelnikova S.E., Baker P.J., Rice D.W., Muench S.P.;
RT "Elucidating the structural basis for differing enzyme inhibitor potency by
RT cryo-EM.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1795-1800(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC 4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC Evidence={ECO:0000269|PubMed:26095028};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128};
CC Note=Binds 2 manganese ions per subunit (PubMed:26095028,
CC PubMed:27717128). Substrate binding triggers a switch in the
CC coordination state of the Mn(2+) active site between six- and five-
CC coordinate species; this switch is critical to prime the active site
CC for catalysis, by facilitating the formation of a high-energy
CC imidazolate intermediate (PubMed:26095028).
CC {ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128};
CC -!- ACTIVITY REGULATION: Weakly inihibited by inorganic phosphate (Pi)
CC (PubMed:26095028). Competitive inhibition by 2-hydroxy-3-(1,2,4-
CC triazol-1-yl) (e.g. C348), a potential herbicide (PubMed:27717128).
CC {ECO:0000269|PubMed:26095028, ECO:0000269|PubMed:27717128}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC {ECO:0000269|PubMed:26095028}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O23346-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10270.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97337; CAB10270.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161540; CAB78533.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83520.1; -; Genomic_DNA.
DR EMBL; AY048237; AAK82500.1; -; mRNA.
DR EMBL; AY094021; AAM16177.1; -; mRNA.
DR PIR; D71412; D71412.
DR RefSeq; NP_567448.1; NM_117577.4. [O23346-1]
DR PDB; 4MU0; X-ray; 1.30 A; A=69-272.
DR PDB; 4MU1; X-ray; 1.50 A; A=54-272.
DR PDB; 4MU3; X-ray; 1.12 A; A=69-272.
DR PDB; 4MU4; X-ray; 1.41 A; A=69-272.
DR PDB; 4QNJ; X-ray; 1.30 A; A=69-272.
DR PDB; 4QNK; X-ray; 1.75 A; A/B/C/D/E/F/G/H=70-272.
DR PDB; 5EKW; X-ray; 1.10 A; A=69-272.
DR PDB; 5EL9; X-ray; 1.10 A; A=69-272.
DR PDB; 5ELW; X-ray; 1.40 A; A=69-272.
DR PDB; 6EZJ; EM; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=69-272.
DR PDBsum; 4MU0; -.
DR PDBsum; 4MU1; -.
DR PDBsum; 4MU3; -.
DR PDBsum; 4MU4; -.
DR PDBsum; 4QNJ; -.
DR PDBsum; 4QNK; -.
DR PDBsum; 5EKW; -.
DR PDBsum; 5EL9; -.
DR PDBsum; 5ELW; -.
DR PDBsum; 6EZJ; -.
DR AlphaFoldDB; O23346; -.
DR SMR; O23346; -.
DR BioGRID; 12446; 1.
DR DIP; DIP-61567N; -.
DR STRING; 3702.AT4G14910.2; -.
DR PaxDb; O23346; -.
DR PRIDE; O23346; -.
DR ProteomicsDB; 230385; -. [O23346-1]
DR EnsemblPlants; AT4G14910.1; AT4G14910.1; AT4G14910. [O23346-1]
DR GeneID; 827149; -.
DR Gramene; AT4G14910.1; AT4G14910.1; AT4G14910. [O23346-1]
DR KEGG; ath:AT4G14910; -.
DR Araport; AT4G14910; -.
DR eggNOG; KOG3143; Eukaryota.
DR HOGENOM; CLU_044308_1_1_1; -.
DR InParanoid; O23346; -.
DR OMA; STHTCDS; -.
DR PhylomeDB; O23346; -.
DR BRENDA; 4.2.1.19; 399.
DR UniPathway; UPA00031; UER00011.
DR PRO; PR:O23346; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23346; baseline and differential.
DR Genevisible; O23346; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR CDD; cd07914; IGPD; 1.
DR Gene3D; 3.30.230.40; -; 2.
DR HAMAP; MF_00076; HisB; 1.
DR InterPro; IPR038494; IGPD_sf.
DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR23133; PTHR23133; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis; Chloroplast;
KW Histidine biosynthesis; Lyase; Manganese; Metal-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..272
FT /note="Imidazoleglycerol-phosphate dehydratase 2,
FT chloroplastic"
FT /id="PRO_0000158254"
FT REGION 24..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27717128,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 112..120
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU3,
FT ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW,
FT ECO:0007744|PDB:5ELW"
FT BINDING 112
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 138..142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU1,
FT ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5ELW"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5ELW"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU3,
FT ECO:0007744|PDB:4MU4, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 210
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5ELW"
FT BINDING 234..242
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU1,
FT ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNK, ECO:0007744|PDB:5EKW,
FT ECO:0007744|PDB:5EL9"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU3, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5ELW"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU0,
FT ECO:0007744|PDB:4MU1, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:4QNJ, ECO:0007744|PDB:4QNK,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT BINDING 264..266
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26095028,
FT ECO:0000269|PubMed:27717128, ECO:0007744|PDB:4MU4,
FT ECO:0007744|PDB:5EKW, ECO:0007744|PDB:5EL9,
FT ECO:0007744|PDB:5ELW"
FT MUTAGEN 73
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26095028"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5EKW"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:5EKW"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5EKW"
FT HELIX 138..156
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5EKW"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:5EKW"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:5EKW"
FT HELIX 233..252
FT /evidence="ECO:0007829|PDB:5EKW"
FT TURN 256..260
FT /evidence="ECO:0007829|PDB:4MU4"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5EKW"
SQ SEQUENCE 272 AA; 29424 MW; 1A2EA7E3D2A5B9B0 CRC64;
MELLSSSPAQ LLRPNLSSRA LLPPRTSIAS SHPPPPRFLV MNSQSQHRPS ISCASPPPGD
NGFPAITTAS PIESARIGEV KRETKETNVS VKINLDGHGV SDSSTGIPFL DHMLDQLASH
GLFDVHVRAT GDTHIDDHHT NEDVALAIGT ALLKALGERK GINRFGDFTA PLDEALIHVS
LDLSGRPYLG YNLEIPTQRV GTYDTQLVEH FFQSLVNTSG MTLHIRQLAG KNSHHIIEAT
FKAFARALRQ ATESDPRRGG TIPSSKGVLS RS
