ID MAP11_HUMAN Reviewed; 386 AA. AC P53582; B4E2E6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2003, sequence version 2. DT 27-MAR-2024, entry version 219. DE RecName: Full=Methionine aminopeptidase 1 {ECO:0000255|HAMAP-Rule:MF_03174}; DE Short=MAP 1 {ECO:0000255|HAMAP-Rule:MF_03174}; DE Short=MetAP 1 {ECO:0000255|HAMAP-Rule:MF_03174}; DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03174}; DE AltName: Full=Peptidase M 1 {ECO:0000255|HAMAP-Rule:MF_03174}; GN Name=METAP1; Synonyms=KIAA0094; 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]. RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. The RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; 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 [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] OF 110-386. RC TISSUE=Placenta; 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 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=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT RP IONS, FUNCTION, AND COFACTOR. RX PubMed=16274222; DOI=10.1021/bi051691k; RA Addlagatta A., Hu X., Liu J.O., Matthews B.W.; RT "Structural basis for the functional differences between type I and type II RT human methionine aminopeptidases."; RL Biochemistry 44:14741-14749(2005). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS RP AND INHIBITORS. RX PubMed=16724298; DOI=10.1002/anie.200600757; RA Hu X., Addlagatta A., Matthews B.W., Liu J.O.; RT "Identification of pyridinylpyrimidines as inhibitors of human methionine RT aminopeptidases."; RL Angew. Chem. Int. Ed. 45:3772-3775(2006). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS RP AND INHIBITORS, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=17114291; DOI=10.1073/pnas.0608389103; RA Hu X., Addlagatta A., Lu J., Matthews B.W., Liu J.O.; RT "Elucidation of the function of type 1 human methionine aminopeptidase RT during cell cycle progression."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18148-18153(2006). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 81-384 IN COMPLEX WITH COBALT IONS RP AND THE INHIBITOR OVALICIN. RX PubMed=16823043; DOI=10.1110/ps.062278006; RA Addlagatta A., Matthews B.W.; RT "Structure of the angiogenesis inhibitor ovalicin bound to its noncognate RT target, human Type 1 methionine aminopeptidase."; RL Protein Sci. 15:1842-1848(2006). CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from CC nascent proteins. The N-terminal methionine is often cleaved when the CC second residue in the primary sequence is small and uncharged (Met- CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression CC through the cell cycle. {ECO:0000269|PubMed:16274222, CC ECO:0000269|PubMed:17114291}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal amino acids, preferentially methionine, CC from peptides and arylamides.; EC=3.4.11.18; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174, CC ECO:0000269|PubMed:17114291}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03174}; CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity CC and a low affinity metal-binding site. The true nature of the CC physiological cofactor is under debate. The enzyme is active with zinc, CC cobalt, manganese or divalent iron ions. Has high activity with zinc; CC zinc cofactor is transferred into the active site region by the ZNG1 CC zinc chaperone. {ECO:0000255|HAMAP-Rule:MF_03174}; CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S CC translational complex. {ECO:0000255|HAMAP-Rule:MF_03174}. CC -!- INTERACTION: CC P53582; O76003: GLRX3; NbExp=3; IntAct=EBI-1051435, EBI-374781; CC P53582; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1051435, EBI-6509505; CC P53582; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1051435, EBI-16439278; CC P53582; Q14596-2: NBR1; NbExp=3; IntAct=EBI-1051435, EBI-11081753; CC P53582; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-1051435, EBI-949255; CC P53582; Q9UGI0: ZRANB1; NbExp=4; IntAct=EBI-1051435, EBI-527853; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03174}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH30054.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA07679.1; Type=Erroneous initiation; 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; D42084; BAA07679.1; ALT_INIT; mRNA. DR EMBL; AK304239; BAG65108.1; -; mRNA. DR EMBL; CH471057; EAX06083.1; -; Genomic_DNA. DR EMBL; BC030054; AAH30054.1; ALT_INIT; mRNA. DR CCDS; CCDS47110.1; -. DR RefSeq; NP_055958.2; NM_015143.2. DR PDB; 2B3H; X-ray; 1.10 A; A=81-384. DR PDB; 2B3K; X-ray; 1.55 A; A=81-384. DR PDB; 2B3L; X-ray; 1.50 A; A=81-384. DR PDB; 2G6P; X-ray; 1.90 A; A=81-384. DR PDB; 2GZ5; X-ray; 1.10 A; A=81-384. DR PDB; 2NQ6; X-ray; 1.50 A; A=81-384. DR PDB; 2NQ7; X-ray; 1.60 A; A=81-384. DR PDB; 4FLI; X-ray; 1.55 A; A=81-386. DR PDB; 4FLJ; X-ray; 1.74 A; A=81-386. DR PDB; 4FLK; X-ray; 1.47 A; A=81-386. DR PDB; 4FLL; X-ray; 1.50 A; A=81-386. DR PDB; 4HXX; X-ray; 2.09 A; A=81-384. DR PDB; 4IKR; X-ray; 1.78 A; A=81-384. DR PDB; 4IKS; X-ray; 1.70 A; A=81-384. DR PDB; 4IKT; X-ray; 1.60 A; A=81-384. DR PDB; 4IKU; X-ray; 1.30 A; A=81-384. DR PDB; 4IU6; X-ray; 1.90 A; A=1-384. DR PDB; 4U1B; X-ray; 1.89 A; A=81-386. DR PDB; 4U69; X-ray; 1.60 A; A=81-386. DR PDB; 4U6C; X-ray; 1.91 A; A=81-386. DR PDB; 4U6E; X-ray; 1.90 A; A=81-386. DR PDB; 4U6J; X-ray; 1.56 A; A=81-386. DR PDB; 4U6W; X-ray; 1.83 A; A=81-386. DR PDB; 4U6Z; X-ray; 1.80 A; A=81-386. DR PDB; 4U70; X-ray; 1.60 A; A=81-386. DR PDB; 4U71; X-ray; 1.80 A; A=81-386. DR PDB; 4U73; X-ray; 1.80 A; A=81-386. DR PDB; 4U75; X-ray; 1.94 A; A=81-386. DR PDB; 4U76; X-ray; 1.87 A; A=81-386. DR PDB; 5YKP; X-ray; 1.68 A; A=81-384. DR PDB; 5YR4; X-ray; 1.82 A; A=81-384. DR PDB; 5YR5; X-ray; 1.60 A; A=81-384. DR PDB; 5YR6; X-ray; 1.75 A; A=81-384. DR PDB; 5YR7; X-ray; 2.06 A; A=81-386. DR PDB; 6LZB; X-ray; 1.29 A; A=81-384. DR PDB; 6LZC; X-ray; 1.35 A; A=81-384. DR PDB; 8P2K; EM; 2.90 A; MA=1-386. DR PDBsum; 2B3H; -. DR PDBsum; 2B3K; -. DR PDBsum; 2B3L; -. DR PDBsum; 2G6P; -. DR PDBsum; 2GZ5; -. DR PDBsum; 2NQ6; -. DR PDBsum; 2NQ7; -. DR PDBsum; 4FLI; -. DR PDBsum; 4FLJ; -. DR PDBsum; 4FLK; -. DR PDBsum; 4FLL; -. DR PDBsum; 4HXX; -. DR PDBsum; 4IKR; -. DR PDBsum; 4IKS; -. DR PDBsum; 4IKT; -. DR PDBsum; 4IKU; -. DR PDBsum; 4IU6; -. DR PDBsum; 4U1B; -. DR PDBsum; 4U69; -. DR PDBsum; 4U6C; -. DR PDBsum; 4U6E; -. DR PDBsum; 4U6J; -. DR PDBsum; 4U6W; -. DR PDBsum; 4U6Z; -. DR PDBsum; 4U70; -. DR PDBsum; 4U71; -. DR PDBsum; 4U73; -. DR PDBsum; 4U75; -. DR PDBsum; 4U76; -. DR PDBsum; 5YKP; -. DR PDBsum; 5YR4; -. DR PDBsum; 5YR5; -. DR PDBsum; 5YR6; -. DR PDBsum; 5YR7; -. DR PDBsum; 6LZB; -. DR PDBsum; 6LZC; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; P53582; -. DR EMDB; EMD-17367; -. DR SMR; P53582; -. DR BioGRID; 116785; 51. DR IntAct; P53582; 25. DR MINT; P53582; -. DR STRING; 9606.ENSP00000296411; -. DR BindingDB; P53582; -. DR ChEMBL; CHEMBL2474; -. DR DrugBank; DB07903; 3-[(2,2-DIMETHYLPROPANOYL)AMINO]-N-1,3-THIAZOL-2-YLPYRIDINE-2-CARBOXAMIDE. DR DrugBank; DB07901; 5-CHLORO-6-METHYL-N-(2-PHENYLETHYL)-2-PYRIDIN-2-YLPYRIMIDIN-4-AMINE. DR DrugBank; DB04324; Ovalicin. DR DrugBank; DB07902; TERT-BUTYL {2-[(1,3-THIAZOL-2-YLAMINO)CARBONYL]PYRIDIN-3-YL}CARBAMATE. DR DrugCentral; P53582; -. DR GuidetoPHARMACOLOGY; 1572; -. DR MEROPS; M24.017; -. DR GlyGen; P53582; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P53582; -. DR PhosphoSitePlus; P53582; -. DR SwissPalm; P53582; -. DR BioMuta; METAP1; -. DR DMDM; 33302602; -. DR EPD; P53582; -. DR jPOST; P53582; -. DR MassIVE; P53582; -. DR MaxQB; P53582; -. DR PaxDb; 9606-ENSP00000296411; -. DR PeptideAtlas; P53582; -. DR ProteomicsDB; 56586; -. DR Pumba; P53582; -. DR Antibodypedia; 25840; 230 antibodies from 25 providers. DR DNASU; 23173; -. DR Ensembl; ENST00000296411.11; ENSP00000296411.6; ENSG00000164024.12. DR GeneID; 23173; -. DR KEGG; hsa:23173; -. DR MANE-Select; ENST00000296411.11; ENSP00000296411.6; NM_015143.3; NP_055958.2. DR UCSC; uc003huf.5; human. DR AGR; HGNC:15789; -. DR CTD; 23173; -. DR DisGeNET; 23173; -. DR GeneCards; METAP1; -. DR HGNC; HGNC:15789; METAP1. DR HPA; ENSG00000164024; Low tissue specificity. DR MIM; 610151; gene. DR neXtProt; NX_P53582; -. DR OpenTargets; ENSG00000164024; -. DR PharmGKB; PA30764; -. DR VEuPathDB; HostDB:ENSG00000164024; -. DR eggNOG; KOG2738; Eukaryota. DR GeneTree; ENSGT00940000158205; -. DR HOGENOM; CLU_015857_2_1_1; -. DR InParanoid; P53582; -. DR OMA; FYGDHAY; -. DR OrthoDB; 5475502at2759; -. DR PhylomeDB; P53582; -. DR TreeFam; TF105753; -. DR BioCyc; MetaCyc:HS08982-MONOMER; -. DR BRENDA; 3.4.11.18; 2681. DR PathwayCommons; P53582; -. DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade. DR SABIO-RK; P53582; -. DR SignaLink; P53582; -. DR BioGRID-ORCS; 23173; 467 hits in 1177 CRISPR screens. DR ChiTaRS; METAP1; human. DR EvolutionaryTrace; P53582; -. DR GeneWiki; METAP1; -. DR GenomeRNAi; 23173; -. DR Pharos; P53582; Tchem. DR PRO; PR:P53582; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P53582; Protein. DR Bgee; ENSG00000164024; Expressed in esophagus squamous epithelium and 209 other cell types or tissues. DR ExpressionAtlas; P53582; baseline and differential. DR GO; GO:0005737; C:cytoplasm; TAS:HGNC-UCL. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004177; F:aminopeptidase activity; IDA:UniProt. DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central. DR GO; GO:0008235; F:metalloexopeptidase activity; TAS:UniProtKB. DR GO; GO:0031365; P:N-terminal protein amino acid modification; TAS:HGNC-UCL. DR GO; GO:0018206; P:peptidyl-methionine modification; TAS:HGNC-UCL. DR GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB. DR GO; GO:0051604; P:protein maturation; IDA:UniProt. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; TAS:HGNC-UCL. DR CDD; cd01086; MetAP1; 1. DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR036005; Creatinase/aminopeptidase-like. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR002467; Pept_M24A_MAP1. DR InterPro; IPR031615; Zfn-C6H2. DR NCBIfam; TIGR00500; met_pdase_I; 1. DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1. DR PANTHER; PTHR43330:SF7; METHIONINE AMINOPEPTIDASE 1; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR Pfam; PF15801; zf-C6H2; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR PROSITE; PS00680; MAP_1; 1. DR PROSITE; PS52013; ZF_C6H2; 1. DR Genevisible; P53582; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; KW Metal-binding; Protease; Reference proteome; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..386 FT /note="Methionine aminopeptidase 1" FT /id="PRO_0000148967" FT ZN_FING 6..59 FT /note="C6H2-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01357" FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174" FT BINDING 203 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N-terminal L-methionine residue" FT /ligand_part_id="ChEBI:CHEBI:64731" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, FT ECO:0000269|PubMed:17114291" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT BINDING 294 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT BINDING 301 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N-terminal L-methionine residue" FT /ligand_part_id="ChEBI:CHEBI:64731" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16724298, ECO:0000269|PubMed:16823043, FT ECO:0000269|PubMed:17114291" FT BINDING 327 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174, FT ECO:0000269|PubMed:16274222, ECO:0000269|PubMed:16724298, FT ECO:0000269|PubMed:16823043, ECO:0000269|PubMed:17114291" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 117..121 FT /evidence="ECO:0007829|PDB:2B3H" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 133..155 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 163..176 FT /evidence="ECO:0007829|PDB:2B3H" FT TURN 182..185 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 191..197 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 216..225 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 228..237 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 243..261 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 271..282 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 297..306 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 323..326 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 329..333 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 346..348 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 354..356 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 358..363 FT /evidence="ECO:0007829|PDB:2B3H" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:2B3H" FT HELIX 381..383 FT /evidence="ECO:0007829|PDB:2B3H" SQ SEQUENCE 386 AA; 43215 MW; 372879013C2BB01D CRC64; MAAVETRVCE TDGCSSEAKL QCPTCIKLGI QGSYFCSQEC FKGSWATHKL LHKKAKDEKA KREVSSWTVE GDINTDPWAG YRYTGKLRPH YPLMPTRPVP SYIQRPDYAD HPLGMSESEQ ALKGTSQIKL LSSEDIEGMR LVCRLAREVL DVAAGMIKPG VTTEEIDHAV HLACIARNCY PSPLNYYNFP KSCCTSVNEV ICHGIPDRRP LQEGDIVNVD ITLYRNGYHG DLNETFFVGE VDDGARKLVQ TTYECLMQAI DAVKPGVRYR ELGNIIQKHA QANGFSVVRS YCGHGIHKLF HTAPNVPHYA KNKAVGVMKS GHVFTIEPMI CEGGWQDETW PDGWTAVTRD GKRSAQFEHT LLVTDTGCEI LTRRLDSARP HFMSQF //