MAP1_STAAM
ID MAP1_STAAM Reviewed; 252 AA.
AC P0A078; Q9KWL1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=SAV1888;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.04 ANGSTROMS) IN COMPLEXES WITH COBALT IONS AND
RP INHIBITOR.
RX PubMed=14998322; DOI=10.1021/jm034188j;
RA Douangamath A., Dale G.E., D'Arcy A., Almstetter M., Eckl R.,
RA Frutos-Hoener A., Henkel B., Illgen K., Nerdinger S., Schulz H.,
RA Mac Sweeney A., Thormann M., Treml A., Pierau S., Wadman S., Oefner C.;
RT "Crystal structures of Staphylococcus aureus methionine aminopeptidase
RT complexed with keto heterocycle and aminoketone inhibitors reveal the
RT formation of a tetrahedral intermediate.";
RL J. Med. Chem. 47:1325-1328(2004).
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}.
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 -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974,
CC ECO:0000269|PubMed:14998322};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
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:14998322};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.
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; BA000017; BAB58050.1; -; Genomic_DNA.
DR RefSeq; WP_000636142.1; NC_002758.2.
DR PDB; 1QXW; X-ray; 1.67 A; A=1-252.
DR PDB; 1QXY; X-ray; 1.04 A; A=1-252.
DR PDB; 1QXZ; X-ray; 1.68 A; A=1-252.
DR PDBsum; 1QXW; -.
DR PDBsum; 1QXY; -.
DR PDBsum; 1QXZ; -.
DR AlphaFoldDB; P0A078; -.
DR SMR; P0A078; -.
DR DrugBank; DB08160; (2S)-2-AMINO-4-(METHYLSULFANYL)-1-(1,3-THIAZOL-2-YL)BUTANE-1,1-DIOL.
DR DrugBank; DB01882; (2s)-2-Amino-4-(Methylsulfanyl)-1-Pyridin-2-Ylbutane-1,1-Diol.
DR DrugBank; DB02408; (3s)-3-Amino-1-(Cyclopropylamino)Heptane-2,2-Diol.
DR MEROPS; M24.036; -.
DR World-2DPAGE; 0002:P0A078; -.
DR PaxDb; P0A078; -.
DR EnsemblBacteria; BAB58050; BAB58050; SAV1888.
DR KEGG; sav:SAV1888; -.
DR HOGENOM; CLU_015857_0_2_9; -.
DR OMA; HWEHSVA; -.
DR PhylomeDB; P0A078; -.
DR BioCyc; SAUR158878:SAV_RS10330-MON; -.
DR EvolutionaryTrace; P0A078; -.
DR PRO; PR:P0A078; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Protease.
FT CHAIN 1..252
FT /note="Methionine aminopeptidase"
FT /id="PRO_0000148955"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:14998322"
FT BINDING 93
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:14998322"
FT BINDING 104
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:14998322"
FT BINDING 104
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:14998322"
FT BINDING 168
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:14998322"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|PubMed:14998322"
FT BINDING 202
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:14998322"
FT BINDING 233
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:14998322"
FT BINDING 233
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:14998322"
FT HELIX 6..29
FT /evidence="ECO:0007829|PDB:1QXY"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1QXY"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:1QXY"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:1QXY"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1QXY"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:1QXY"
SQ SEQUENCE 252 AA; 27502 MW; 3E42E623286B537B CRC64;
MIVKTEEELQ ALKEIGYICA KVRNTMQAAT KPGITTKELD NIAKELFEEY GAISAPIHDE
NFPGQTCISV NEEVAHGIPS KRVIREGDLV NIDVSALKNG YYADTGISFV VGESDDPMKQ
KVCDVATMAF ENAIAKVKPG TKLSNIGKAV HNTARQNDLK VIKNLTGHGV GLSLHEAPAH
VLNYFDPKDK TLLTEGMVLA IEPFISSNAS FVTEGKNEWA FETSDKSFVA QIEHTVIVTK
DGPILTTKIE EE
