RPE_HUMAN
ID RPE_HUMAN Reviewed; 228 AA.
AC Q96AT9; A8K4S0; B4E016; C9JPQ7; O43767; Q53TV9; Q8N215; Q96N34; Q9BSB5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ribulose-phosphate 3-epimerase;
DE EC=5.1.3.1 {ECO:0000269|PubMed:20923965};
DE AltName: Full=Ribulose-5-phosphate-3-epimerase;
GN Name=RPE; ORFNames=HUSSY-17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 55-228 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=11124703;
RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA Zimbello R., Lanfranchi G., Valle G.;
RT "Characterization of 16 novel human genes showing high similarity to yeast
RT sequences.";
RL Yeast 18:69-80(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8] {ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEXES WITH IRON ION;
RP D-RIBULOSE 5-PHOSPHATE AND D-XYLULOSE 5-PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, MUTAGENESIS OF SER-10; LEU-12; HIS-35; ASP-37; MET-39;
RP HIS-70; MET-72; MET-141 AND ASP-175, PATHWAY, AND ACTIVE SITE.
RX PubMed=20923965; DOI=10.1096/fj.10-171207;
RA Liang W., Ouyang S., Shaw N., Joachimiak A., Zhang R., Liu Z.J.;
RT "Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new
RT insights from structural and biochemical studies on human RPE.";
RL FASEB J. 25:497-504(2011).
RN [9] {ECO:0007744|PDB:3QC3}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-224 IN COMPLEX WITH NICKEL;
RP ZINC AND IRON IONS.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a D-ribulose-5-phosphate-3-epimerase (NP_954699) from
RT Homo sapiens at 2.20 A resolution.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000269|PubMed:20923965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000269|PubMed:20923965};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20923965};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20923965};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20923965};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:20923965};
CC Note=Binds 1 divalent metal cation per subunit. Active with Fe(2+), and
CC probably also with Mn(2+), Zn(2+) and Co(2+).
CC {ECO:0000269|PubMed:20923965};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000269|PubMed:20923965}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC Q96AT9; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-372480, EBI-742388;
CC Q96AT9; Q96AT9: RPE; NbExp=6; IntAct=EBI-372480, EBI-372480;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96AT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AT9-2; Sequence=VSP_008317, VSP_008318;
CC Name=3;
CC IsoId=Q96AT9-3; Sequence=VSP_047117, VSP_008318;
CC Name=4;
CC IsoId=Q96AT9-4; Sequence=VSP_055265;
CC Name=5;
CC IsoId=Q96AT9-5; Sequence=VSP_047117;
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71076.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC04212.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK056028; BAB71076.1; ALT_FRAME; mRNA.
DR EMBL; AK093658; BAC04212.1; ALT_FRAME; mRNA.
DR EMBL; AK291035; BAF83724.1; -; mRNA.
DR EMBL; AK303184; BAG64278.1; -; mRNA.
DR EMBL; AC007038; AAX93087.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70473.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70474.1; -; Genomic_DNA.
DR EMBL; BC005148; AAH05148.2; -; mRNA.
DR EMBL; BC016764; AAH16764.1; -; mRNA.
DR EMBL; BC072401; AAH72401.1; -; mRNA.
DR EMBL; AJ224326; CAA11895.1; -; mRNA.
DR CCDS; CCDS2388.1; -. [Q96AT9-1]
DR CCDS; CCDS42810.1; -. [Q96AT9-3]
DR CCDS; CCDS63107.1; -. [Q96AT9-4]
DR CCDS; CCDS63108.1; -. [Q96AT9-5]
DR RefSeq; NP_001265211.1; NM_001278282.1. [Q96AT9-3]
DR RefSeq; NP_001265212.1; NM_001278283.1. [Q96AT9-3]
DR RefSeq; NP_001265214.1; NM_001278285.1. [Q96AT9-4]
DR RefSeq; NP_001265215.1; NM_001278286.1. [Q96AT9-5]
DR RefSeq; NP_001265217.1; NM_001278288.1. [Q96AT9-5]
DR RefSeq; NP_001265218.1; NM_001278289.1.
DR RefSeq; NP_001305855.1; NM_001318926.1.
DR RefSeq; NP_001305856.1; NM_001318927.1.
DR RefSeq; NP_001305857.1; NM_001318928.1.
DR RefSeq; NP_001305858.1; NM_001318929.1.
DR RefSeq; NP_001305859.1; NM_001318930.1. [Q96AT9-5]
DR RefSeq; NP_001305860.1; NM_001318931.1. [Q96AT9-5]
DR RefSeq; NP_008847.1; NM_006916.2. [Q96AT9-3]
DR RefSeq; NP_954699.1; NM_199229.2. [Q96AT9-1]
DR RefSeq; XP_006712740.1; XM_006712677.3. [Q96AT9-5]
DR PDB; 3OVP; X-ray; 1.70 A; A/B=1-228.
DR PDB; 3OVQ; X-ray; 2.00 A; A/B=1-228.
DR PDB; 3OVR; X-ray; 1.95 A; A/B=1-228.
DR PDB; 3QC3; X-ray; 2.20 A; A/B=1-224.
DR PDBsum; 3OVP; -.
DR PDBsum; 3OVQ; -.
DR PDBsum; 3OVR; -.
DR PDBsum; 3QC3; -.
DR AlphaFoldDB; Q96AT9; -.
DR SMR; Q96AT9; -.
DR BioGRID; 112040; 55.
DR IntAct; Q96AT9; 7.
DR STRING; 9606.ENSP00000352401; -.
DR DrugBank; DB00153; Ergocalciferol.
DR GlyGen; Q96AT9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96AT9; -.
DR PhosphoSitePlus; Q96AT9; -.
DR BioMuta; RPE; -.
DR DMDM; 34924986; -.
DR EPD; Q96AT9; -.
DR jPOST; Q96AT9; -.
DR MassIVE; Q96AT9; -.
DR MaxQB; Q96AT9; -.
DR PaxDb; Q96AT9; -.
DR PeptideAtlas; Q96AT9; -.
DR PRIDE; Q96AT9; -.
DR ProteomicsDB; 11146; -.
DR ProteomicsDB; 5637; -.
DR ProteomicsDB; 62553; -.
DR ProteomicsDB; 75997; -. [Q96AT9-1]
DR ProteomicsDB; 75998; -. [Q96AT9-2]
DR TopDownProteomics; Q96AT9-1; -. [Q96AT9-1]
DR TopDownProteomics; Q96AT9-2; -. [Q96AT9-2]
DR Antibodypedia; 34203; 132 antibodies from 25 providers.
DR DNASU; 6120; -.
DR Ensembl; ENST00000354506.10; ENSP00000346501.7; ENSG00000197713.15. [Q96AT9-4]
DR Ensembl; ENST00000359429.11; ENSP00000352401.6; ENSG00000197713.15. [Q96AT9-1]
DR Ensembl; ENST00000411934.6; ENSP00000389411.1; ENSG00000197713.15. [Q96AT9-5]
DR Ensembl; ENST00000429921.5; ENSP00000401838.1; ENSG00000197713.15. [Q96AT9-3]
DR Ensembl; ENST00000436630.6; ENSP00000403808.2; ENSG00000197713.15. [Q96AT9-3]
DR Ensembl; ENST00000438204.6; ENSP00000402061.1; ENSG00000197713.15. [Q96AT9-5]
DR Ensembl; ENST00000454822.5; ENSP00000394455.1; ENSG00000197713.15. [Q96AT9-3]
DR GeneID; 6120; -.
DR KEGG; hsa:6120; -.
DR MANE-Select; ENST00000359429.11; ENSP00000352401.6; NM_199229.3; NP_954699.1.
DR UCSC; uc002vdn.5; human. [Q96AT9-1]
DR CTD; 6120; -.
DR DisGeNET; 6120; -.
DR GeneCards; RPE; -.
DR HGNC; HGNC:10293; RPE.
DR HPA; ENSG00000197713; Low tissue specificity.
DR MIM; 180480; gene.
DR neXtProt; NX_Q96AT9; -.
DR OpenTargets; ENSG00000197713; -.
DR PharmGKB; PA34654; -.
DR VEuPathDB; HostDB:ENSG00000197713; -.
DR eggNOG; KOG3111; Eukaryota.
DR GeneTree; ENSGT00390000001447; -.
DR InParanoid; Q96AT9; -.
DR OMA; WLQVDGG; -.
DR OrthoDB; 1554029at2759; -.
DR PhylomeDB; Q96AT9; -.
DR TreeFam; TF300157; -.
DR BRENDA; 5.1.3.1; 2681.
DR PathwayCommons; Q96AT9; -.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR SignaLink; Q96AT9; -.
DR SIGNOR; Q96AT9; -.
DR BioGRID-ORCS; 6120; 622 hits in 1083 CRISPR screens.
DR ChiTaRS; RPE; human.
DR EvolutionaryTrace; Q96AT9; -.
DR GeneWiki; RPE_(gene); -.
DR GenomeRNAi; 6120; -.
DR Pharos; Q96AT9; Tbio.
DR PRO; PR:Q96AT9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96AT9; protein.
DR Bgee; ENSG00000197713; Expressed in adrenal tissue and 191 other tissues.
DR ExpressionAtlas; Q96AT9; baseline and differential.
DR Genevisible; Q96AT9; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IDA:UniProtKB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01163; rpe; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism;
KW Cobalt; Iron; Isomerase; Manganese; Metal-binding; Reference proteome;
KW Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..228
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171587"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVR"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:20923965, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ,
FT ECO:0007744|PDB:3OVR, ECO:0007744|PDB:3QC3"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:20923965, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ,
FT ECO:0007744|PDB:3OVR, ECO:0007744|PDB:3QC3"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:20923965, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ,
FT ECO:0007744|PDB:3OVR, ECO:0007744|PDB:3QC3"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:20923965, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:3OVP, ECO:0007744|PDB:3OVQ,
FT ECO:0007744|PDB:3OVR, ECO:0007744|PDB:3QC3"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20923965,
FT ECO:0007744|PDB:3OVQ, ECO:0007744|PDB:3OVR"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047117"
FT VAR_SEQ 43..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008317"
FT VAR_SEQ 114
FT /note="K -> KSCSVTQAEVQWHSQGPLQ (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008318"
FT VAR_SEQ 160..188
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055265"
FT MUTAGEN 10
FT /note="S->A: Nearly abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 12
FT /note="L->A: Reduces enzyme activity by half."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 35
FT /note="H->A: Alters protein structure. Nearly abolishes
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 37
FT /note="D->A: Alters protein structure. Nearly abolishes
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 39
FT /note="M->A: Lowers enzyme activity by 10%."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 70
FT /note="H->A: Alters protein structure."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 72
FT /note="M->A: Reduces enzyme activity by half."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 141
FT /note="M->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:20923965"
FT MUTAGEN 175
FT /note="D->A: Alters protein structure."
FT /evidence="ECO:0000269|PubMed:20923965"
FT CONFLICT 180
FT /note="P -> L (in Ref. 1; BAC04212)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:3OVP"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:3OVP"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:3OVP"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:3OVP"
FT HELIX 206..223
FT /evidence="ECO:0007829|PDB:3OVP"
SQ SEQUENCE 228 AA; 24928 MW; 447130018AC52331 CRC64;
MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ
LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YTFHLEATEN PGALIKDIRE NGMKVGLAIK
PGTSVEYLAP WANQIDMALV MTVEPGFGGQ KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP
DTVHKCAEAG ANMIVSGSAI MRSEDPRSVI NLLRNVCSEA AQKRSLDR
