MAP1_ECOLI
ID MAP1_ECOLI Reviewed; 264 AA.
AC P0AE18; P07906;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974};
DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974};
GN Name=map {ECO:0000255|HAMAP-Rule:MF_01974};
GN OrderedLocusNames=b0168, JW0163;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-64, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=3027045; DOI=10.1128/jb.169.2.751-757.1987;
RA Ben-Bassat A., Bauer K., Chang S.-Y., Myambo K., Boosman A., Chang S.;
RT "Processing of the initiation methionine from proteins: properties of the
RT Escherichia coli methionine aminopeptidase and its gene structure.";
RL J. Bacteriol. 169:751-757(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10460163; DOI=10.1021/bi990872h;
RA D'souza V.M., Holz R.C.;
RT "The methionyl aminopeptidase from Escherichia coli can function as an
RT iron(II) enzyme.";
RL Biochemistry 38:11079-11085(1999).
RN [8]
RP COFACTOR.
RX PubMed=10736182; DOI=10.1021/bi9925827;
RA D'souza V.M., Bennett B., Copik A.J., Holz R.C.;
RT "Divalent metal binding properties of the methionyl aminopeptidase from
RT Escherichia coli.";
RL Biochemistry 39:3817-3826(2000).
RN [9]
RP MUTAGENESIS OF HIS-178, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12755633; DOI=10.1021/bi027327s;
RA Copik A.J., Swierczek S.I., Lowther W.T., D'souza V.M., Matthews B.W.,
RA Holz R.C.;
RT "Kinetic and spectroscopic characterization of the H178A methionyl
RT aminopeptidase from Escherichia coli.";
RL Biochemistry 42:6283-6292(2003).
RN [10]
RP MUTAGENESIS OF HIS-79, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18855426; DOI=10.1021/bi801499g;
RA Watterson S.J., Mitra S., Swierczek S.I., Bennett B., Holz R.C.;
RT "Kinetic and spectroscopic analysis of the catalytic role of H79 in the
RT methionine aminopeptidase from Escherichia coli.";
RL Biochemistry 47:11885-11893(2008).
RN [11]
RP MUTAGENESIS OF ASP-97, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19019076; DOI=10.1111/j.1742-4658.2008.06749.x;
RA Mitra S., Job K.M., Meng L., Bennett B., Holz R.C.;
RT "Analyzing the catalytic role of Asp97 in the methionine aminopeptidase
RT from Escherichia coli.";
RL FEBS J. 275:6248-6259(2008).
RN [12]
RP COFACTOR.
RX PubMed=20017927; DOI=10.1186/1471-2091-10-32;
RA Chai S.C., Ye Q.Z.;
RT "Analysis of the stoichiometric metal activation of methionine
RT aminopeptidase.";
RL BMC Biochem. 10:32-32(2009).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20521764; DOI=10.1021/bi1005464;
RA Xiao Q., Zhang F., Nacev B.A., Liu J.O., Pei D.;
RT "Protein N-terminal processing: substrate specificity of Escherichia coli
RT and human methionine aminopeptidases.";
RL Biochemistry 49:5588-5599(2010).
RN [14]
RP COFACTOR.
RX PubMed=22112844; DOI=10.1016/j.jinorgbio.2011.09.020;
RA Sule N., Singh R.K., Zhao P., Srivastava D.K.;
RT "Probing the metal ion selectivity in methionine aminopeptidase via changes
RT in the luminescence properties of the enzyme bound europium ion.";
RL J. Inorg. Biochem. 106:84-89(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8471602; DOI=10.1021/bi00066a009;
RA Roderick S.L., Mathews B.W.;
RT "Structure of the cobalt-dependent methionine aminopeptidase from
RT Escherichia coli: a new type of proteolytic enzyme.";
RL Biochemistry 32:3907-3912(1993).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SODIUM; COBALT IONS
RP AND INHIBITOR, COFACTOR, AND MUTAGENESIS OF HIS-79 AND HIS-178.
RX PubMed=10387007; DOI=10.1021/bi990684r;
RA Lowther W.T., Orville A.M., Madden D.T., Lim S., Rich D.H., Matthews B.W.;
RT "Escherichia coli methionine aminopeptidase: implications of
RT crystallographic analyses of the native, mutant, and inhibited enzymes for
RT the mechanism of catalysis.";
RL Biochemistry 38:7678-7688(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH COBALT IONS;
RP PRODUCT AND TRANSITION STATE ANALOGS.
RX PubMed=10555963; DOI=10.1021/bi991711g;
RA Lowther W.T., Zhang Y., Sampson P.B., Honek J.F., Matthews B.W.;
RT "Insights into the mechanism of Escherichia coli methionine aminopeptidase
RT from the structural analysis of reaction products and phosphorus-based
RT transition-state analogues.";
RL Biochemistry 38:14810-14819(1999).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 4-264 IN COMPLEX WITH MANGANESE
RP AND A TRANSITION STATE ANALOG, AND COFACTOR.
RX PubMed=16769889; DOI=10.1073/pnas.0602433103;
RA Ye Q.Z., Xie S.X., Ma Z.Q., Huang M., Hanzlik R.P.;
RT "Structural basis of catalysis by monometalated methionine
RT aminopeptidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9470-9475(2006).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 2-264 IN COMPLEXES WITH MANGANESE
RP IONS AND INHIBITORS.
RX PubMed=18093325; DOI=10.1186/1472-6807-7-84;
RA Ma Z.-Q., Xie S.-X., Huang Q.-Q., Nan F.-J., Hurley T.D., Ye Q.-Z.;
RT "Structural analysis of inhibition of E. coli methionine aminopeptidase:
RT implication of loop adaptability in selective inhibition of bacterial
RT enzymes.";
RL BMC Struct. Biol. 7:84-84(2007).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 2-264 IN COMPLEXES WITH COBALT
RP IONS; METHIONINE OR INHIBITORS OF THE PYRAZOLE DIAMINE TYPE, AND CATALYTIC
RP ACTIVITY.
RX PubMed=17120228; DOI=10.1002/prot.21207;
RA Evdokimov A.G., Pokross M., Walter R.L., Mekel M., Barnett B.L.,
RA Amburgey J., Seibel W.L., Soper S.J., Djung J.F., Fairweather N., Diven C.,
RA Rastogi V., Grinius L., Klanke C., Siehnel R., Twinem T., Andrews R.,
RA Curnow A.;
RT "Serendipitous discovery of novel bacterial methionine aminopeptidase
RT inhibitors.";
RL Proteins 66:538-546(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 4-264 IN COMPLEXES WITH
RP CATECHOL-CONTAINING INHIBITORS AND IRON IONS, AND COFACTOR.
RX PubMed=18785729; DOI=10.1021/jm8005788;
RA Wang W.-L., Chai S.C., Huang M., He H.-Z., Hurley T.D., Ye Q.-Z.;
RT "Discovery of inhibitors of Escherichia coli methionine aminopeptidase with
RT the Fe(II)-form selectivity and antibacterial activity.";
RL J. Med. Chem. 51:6110-6120(2008).
CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC N-terminal methionine is often cleaved when the second residue in the
CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC Thr, or Val). Requires deformylation of the N(alpha)-formylated
CC initiator methionine before it can be hydrolyzed. {ECO:0000255|HAMAP-
CC Rule:MF_01974, ECO:0000269|PubMed:20521764,
CC ECO:0000269|PubMed:3027045}.
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_01974,
CC ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:20521764,
CC ECO:0000269|PubMed:3027045};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974,
CC ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10460163,
CC ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:10736182,
CC ECO:0000269|PubMed:17120228, ECO:0000269|PubMed:20017927};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974,
CC ECO:0000269|PubMed:10460163};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974,
CC ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:16769889,
CC ECO:0000269|PubMed:18093325};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974,
CC ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:10736182,
CC ECO:0000269|PubMed:18785729, ECO:0000269|PubMed:22112844};
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
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000255|HAMAP-Rule:MF_01974, ECO:0000269|PubMed:10460163,
CC ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:18785729,
CC ECO:0000269|PubMed:22112844};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:10387007};
CC Note=Binds 1 sodium ion per subunit. The sodium ion has a structural
CC role. {ECO:0000269|PubMed:10387007};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for a Met-Gly-Met-Met peptide (for the Fe(2+)-complexed
CC enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633,
CC ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076};
CC KM=1.3 mM for a Met-Gly-Met-Met peptide (for the Mn(2+)-complexed
CC enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633,
CC ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076};
CC KM=3.2 mM for a Met-Gly-Met-Met peptide (for the Co(2+)-complexed
CC enzyme) {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633,
CC ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076};
CC Vmax=55 umol/min/mg enzyme (for the Fe(2+)-complexed enzyme)
CC {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633,
CC ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076};
CC Vmax=77 umol/min/mg enzyme (for the Co(2+)-complexed enzyme)
CC {ECO:0000269|PubMed:10460163, ECO:0000269|PubMed:12755633,
CC ECO:0000269|PubMed:18855426, ECO:0000269|PubMed:19019076};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974,
CC ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:16769889}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}.
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DR EMBL; M15106; AAA24112.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08597.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73279.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96743.1; -; Genomic_DNA.
DR PIR; A27761; DPECM.
DR RefSeq; NP_414710.1; NC_000913.3.
DR RefSeq; WP_001018194.1; NZ_STEB01000032.1.
DR PDB; 1C21; X-ray; 1.80 A; A=2-264.
DR PDB; 1C22; X-ray; 1.75 A; A=2-264.
DR PDB; 1C23; X-ray; 2.00 A; A=2-264.
DR PDB; 1C24; X-ray; 1.70 A; A=2-264.
DR PDB; 1C27; X-ray; 1.95 A; A=2-264.
DR PDB; 1MAT; X-ray; 2.40 A; A=1-264.
DR PDB; 1XNZ; X-ray; 1.52 A; A=1-264.
DR PDB; 1YVM; X-ray; 1.60 A; A=1-264.
DR PDB; 2BB7; X-ray; 1.70 A; A=1-264.
DR PDB; 2EVC; X-ray; 1.60 A; A=1-264.
DR PDB; 2EVM; X-ray; 1.70 A; A=1-264.
DR PDB; 2EVO; X-ray; 1.70 A; A/B=1-264.
DR PDB; 2GG0; X-ray; 1.28 A; A=2-264.
DR PDB; 2GG2; X-ray; 1.00 A; A=2-264.
DR PDB; 2GG3; X-ray; 1.45 A; A=2-264.
DR PDB; 2GG5; X-ray; 2.12 A; A=2-264.
DR PDB; 2GG7; X-ray; 1.12 A; A=2-264.
DR PDB; 2GG8; X-ray; 1.80 A; A=2-264.
DR PDB; 2GG9; X-ray; 1.05 A; A=2-264.
DR PDB; 2GGB; X-ray; 2.13 A; A=2-264.
DR PDB; 2GGC; X-ray; 1.00 A; A=2-264.
DR PDB; 2GTX; X-ray; 2.00 A; A/B=4-264.
DR PDB; 2GU4; X-ray; 1.80 A; A/B=2-264.
DR PDB; 2GU5; X-ray; 1.60 A; A/B=2-264.
DR PDB; 2GU6; X-ray; 1.70 A; A/B=2-264.
DR PDB; 2GU7; X-ray; 2.00 A; A/B=2-264.
DR PDB; 2MAT; X-ray; 1.90 A; A=1-264.
DR PDB; 2P98; X-ray; 1.70 A; A=2-262.
DR PDB; 2P99; X-ray; 1.80 A; A=2-262.
DR PDB; 2P9A; X-ray; 1.60 A; A=2-263.
DR PDB; 2Q92; X-ray; 1.90 A; A=2-263.
DR PDB; 2Q93; X-ray; 1.60 A; A=2-264.
DR PDB; 2Q94; X-ray; 1.63 A; A=2-263.
DR PDB; 2Q95; X-ray; 1.70 A; A=2-264.
DR PDB; 2Q96; X-ray; 1.60 A; A=2-264.
DR PDB; 3D27; X-ray; 2.20 A; A=4-264.
DR PDB; 3MAT; X-ray; 2.00 A; A=1-264.
DR PDB; 4MAT; X-ray; 2.00 A; A=1-264.
DR PDB; 4Z7M; X-ray; 1.43 A; A/B=2-262.
DR PDB; 6IZ7; EM; 11.80 A; P=1-264.
DR PDB; 6IZI; EM; 11.80 A; Q=1-264.
DR PDB; 6J0A; EM; 14.20 A; P=1-264.
DR PDBsum; 1C21; -.
DR PDBsum; 1C22; -.
DR PDBsum; 1C23; -.
DR PDBsum; 1C24; -.
DR PDBsum; 1C27; -.
DR PDBsum; 1MAT; -.
DR PDBsum; 1XNZ; -.
DR PDBsum; 1YVM; -.
DR PDBsum; 2BB7; -.
DR PDBsum; 2EVC; -.
DR PDBsum; 2EVM; -.
DR PDBsum; 2EVO; -.
DR PDBsum; 2GG0; -.
DR PDBsum; 2GG2; -.
DR PDBsum; 2GG3; -.
DR PDBsum; 2GG5; -.
DR PDBsum; 2GG7; -.
DR PDBsum; 2GG8; -.
DR PDBsum; 2GG9; -.
DR PDBsum; 2GGB; -.
DR PDBsum; 2GGC; -.
DR PDBsum; 2GTX; -.
DR PDBsum; 2GU4; -.
DR PDBsum; 2GU5; -.
DR PDBsum; 2GU6; -.
DR PDBsum; 2GU7; -.
DR PDBsum; 2MAT; -.
DR PDBsum; 2P98; -.
DR PDBsum; 2P99; -.
DR PDBsum; 2P9A; -.
DR PDBsum; 2Q92; -.
DR PDBsum; 2Q93; -.
DR PDBsum; 2Q94; -.
DR PDBsum; 2Q95; -.
DR PDBsum; 2Q96; -.
DR PDBsum; 3D27; -.
DR PDBsum; 3MAT; -.
DR PDBsum; 4MAT; -.
DR PDBsum; 4Z7M; -.
DR PDBsum; 6IZ7; -.
DR PDBsum; 6IZI; -.
DR PDBsum; 6J0A; -.
DR AlphaFoldDB; P0AE18; -.
DR SMR; P0AE18; -.
DR BioGRID; 4262194; 76.
DR DIP; DIP-48040N; -.
DR IntAct; P0AE18; 25.
DR STRING; 511145.b0168; -.
DR BindingDB; P0AE18; -.
DR ChEMBL; CHEMBL3423; -.
DR DrugBank; DB08668; 3-(5-Amino-3-imino-3H-pyrazol-4-ylazo)-benzoic acid.
DR DrugBank; DB08718; 4-(3-ethylthiophen-2-yl)benzene-1,2-diol.
DR DrugBank; DB08667; 4-(4-fluoro-phenylazo)-5-imino-5H-pyrazol-3-ylamine.
DR DrugBank; DB07758; 5-(2,5-DICHLOROPHENYL)-2-FUROIC ACID.
DR DrugBank; DB07305; 5-(2-CHLORO-4-NITROPHENYL)-2-FUROIC ACID.
DR DrugBank; DB07308; 5-(2-CHLOROBENZYL)-2-FUROIC ACID.
DR DrugBank; DB08757; 5-(2-chlorophenyl)furan-2-carbohydrazide.
DR DrugBank; DB02909; 5-(2-Chlorophenyl)Furan-2-Carboxylic Acid.
DR DrugBank; DB07407; 5-(2-METHOXYPHENYL)-2-FUROIC ACID.
DR DrugBank; DB07408; 5-(2-NITROPHENYL)-2-FUROIC ACID.
DR DrugBank; DB07304; 5-[2-(TRIFLUOROMETHOXY)PHENYL]-2-FUROIC ACID.
DR DrugBank; DB07759; 5-[2-(TRIFLUOROMETHYL)PHENYL]-2-FUROIC ACID.
DR DrugBank; DB08671; 5-Imino-4-(2-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamine.
DR DrugBank; DB08666; 5-imino-4-(3-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamine.
DR DrugBank; DB08758; IMIDAZO[2,1-A]ISOQUINOLINE-2-CARBOHYDRAZIDE.
DR DrugBank; DB04015; Methionine Phosphinate.
DR DrugBank; DB02151; Methionine Phosphonate.
DR DrugBank; DB08670; METHYL N-[(2S,3R)-3-AMINO-2-HYDROXY-3-(4-ISOPROPYLPHENYL)PROPANOYL]-D-ALANYL-D-LEUCINATE.
DR DrugBank; DB08669; METHYL N-[(2S,3R)-3-AMINO-2-HYDROXY-3-(4-METHYLPHENYL)PROPANOYL]-D-ALANYL-D-LEUCINATE.
DR DrugBank; DB08451; N-(QUINOLIN-8-YL)METHANESULFONAMIDE.
DR DrugBank; DB07591; N1-CYCLOPENTYL-N2-(THIAZOL-2-YL)OXALAMIDE.
DR DrugBank; DB02088; Norleucine Phosphonate.
DR DrugBank; DB03799; Trifluoromethionine.
DR DrugCentral; P0AE18; -.
DR MEROPS; M24.001; -.
DR SWISS-2DPAGE; P0AE18; -.
DR jPOST; P0AE18; -.
DR PaxDb; P0AE18; -.
DR PRIDE; P0AE18; -.
DR EnsemblBacteria; AAC73279; AAC73279; b0168.
DR EnsemblBacteria; BAB96743; BAB96743; BAB96743.
DR GeneID; 66671544; -.
DR GeneID; 947882; -.
DR KEGG; ecj:JW0163; -.
DR KEGG; eco:b0168; -.
DR PATRIC; fig|1411691.4.peg.2113; -.
DR EchoBASE; EB0565; -.
DR eggNOG; COG0024; Bacteria.
DR HOGENOM; CLU_015857_0_0_6; -.
DR InParanoid; P0AE18; -.
DR OMA; GDHAYTF; -.
DR PhylomeDB; P0AE18; -.
DR BioCyc; EcoCyc:EG10570-MON; -.
DR BioCyc; MetaCyc:EG10570-MON; -.
DR BRENDA; 3.4.11.18; 2026.
DR SABIO-RK; P0AE18; -.
DR EvolutionaryTrace; P0AE18; -.
DR PRO; PR:P0AE18; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IDA:EcoCyc.
DR GO; GO:0070084; P:protein initiator methionine removal; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 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 Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Direct protein sequencing; Hydrolase;
KW Metal-binding; Protease; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3027045"
FT CHAIN 2..264
FT /note="Methionine aminopeptidase"
FT /id="PRO_0000148937"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889,
FT ECO:0000269|PubMed:17120228"
FT BINDING 97
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT BINDING 171
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10555963, ECO:0000269|PubMed:16769889,
FT ECO:0000269|PubMed:17120228"
FT BINDING 204
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:10387007, ECO:0000269|PubMed:10555963,
FT ECO:0000269|PubMed:16769889, ECO:0000269|PubMed:17120228,
FT ECO:0000269|PubMed:18093325, ECO:0000269|PubMed:18785729"
FT MUTAGEN 79
FT /note="H->A: Reduces activity 100000-fold for the Co(2+)-
FT complexed enzyme, but only 2.6-fold for the Mn(2+)-
FT complexed enzyme."
FT /evidence="ECO:0000269|PubMed:10387007,
FT ECO:0000269|PubMed:18855426"
FT MUTAGEN 97
FT /note="D->A,E,N: Reduces activity 50- to 580-fold depending
FT on the metal ion bound. Binds only one equivalent of the
FT divalent metal cation with affinities identical to the
FT wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:19019076"
FT MUTAGEN 178
FT /note="H->A: Reduces activity 9000-fold for the Co(2+)-
FT complexed enzyme. Binds only one equivalent of the divalent
FT metal cation with affinities identical to the wild-type
FT enzyme."
FT /evidence="ECO:0000269|PubMed:10387007,
FT ECO:0000269|PubMed:12755633"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:2GG2"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2GG2"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2GG2"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2GGB"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:2GG2"
FT HELIX 146..159
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2GG9"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2EVM"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2GG2"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2GG2"
SQ SEQUENCE 264 AA; 29331 MW; F2D0B57715A67851 CRC64;
MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL
GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI
MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE
PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV
TDNGCEILTL RKDDTIPAII SHDE
