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 22-FEB-2023, entry version 178. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 57. 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 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; 133 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 AGR; HGNC:10293; -. 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; 101513at2759; -. 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; 651 hits in 1166 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; Aldolase class I; 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; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1. DR PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE-RELATED; 1. DR Pfam; PF00834; Ribul_P_3_epim; 1. DR PIRSF; PIRSF001461; RPE; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 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 //