MAP1_RICPR
ID MAP1_RICPR Reviewed; 259 AA.
AC Q9ZCD3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=RP824;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 3-249 IN COMPLEX WITH MANGANESE
RP IONS.
RG Seattle structural genomics center for infectious disease (SSGCID);
RA Edwards T.E., Abendroth J., Sankaran B.;
RT "Crystal structure of methionine aminopeptidase from Rickettsia
RT prowazekii.";
RL Submitted (APR-2010) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 3-259 IN COMPLEX WITH MANGANESE
RP IONS AND METHIONINE.
RG Seattle Structural Genomics Center for Infectious Disease (SSGCID);
RA Edwards T.E., Abendroth J., Arakaki T., Sankaran B.;
RT "Crystal structure of methionine aminopeptidase from Rickettsia prowazekii
RT bound to methionine.";
RL Submitted (MAY-2010) to the PDB data bank.
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 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, ECO:0000269|Ref.2,
CC ECO:0000269|Ref.3};
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};
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; AJ235273; CAA15249.1; -; Genomic_DNA.
DR PIR; A71644; A71644.
DR RefSeq; NP_221173.1; NC_000963.1.
DR RefSeq; WP_004599671.1; NC_000963.1.
DR PDB; 3MR1; X-ray; 2.00 A; A/B/C/D=3-249.
DR PDB; 3MX6; X-ray; 1.70 A; A/B=3-259.
DR PDBsum; 3MR1; -.
DR PDBsum; 3MX6; -.
DR AlphaFoldDB; Q9ZCD3; -.
DR SMR; Q9ZCD3; -.
DR STRING; 272947.RP824; -.
DR MEROPS; M24.001; -.
DR EnsemblBacteria; CAA15249; CAA15249; CAA15249.
DR GeneID; 57569946; -.
DR KEGG; rpr:RP824; -.
DR PATRIC; fig|272947.5.peg.860; -.
DR eggNOG; COG0024; Bacteria.
DR HOGENOM; CLU_015857_0_0_5; -.
DR OMA; GDHAYTF; -.
DR BRENDA; 3.4.11.18; 5447.
DR EvolutionaryTrace; Q9ZCD3; -.
DR Proteomes; UP000002480; 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.
DR PROSITE; PS00680; MAP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Protease;
KW Reference proteome.
FT CHAIN 1..259
FT /note="Methionine aminopeptidase"
FT /id="PRO_0000148950"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 95
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|Ref.2, ECO:0000269|Ref.3"
FT BINDING 106
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|Ref.2, ECO:0000269|Ref.3"
FT BINDING 106
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|Ref.2, ECO:0000269|Ref.3"
FT BINDING 169
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|Ref.2, ECO:0000269|Ref.3"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974,
FT ECO:0000269|Ref.3"
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|Ref.2, ECO:0000269|Ref.3"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 234
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|Ref.2, ECO:0000269|Ref.3"
FT BINDING 234
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|Ref.2, ECO:0000269|Ref.3"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:3MX6"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:3MX6"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:3MX6"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3MX6"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:3MX6"
FT HELIX 118..136
FT /evidence="ECO:0007829|PDB:3MX6"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3MX6"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3MX6"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:3MX6"
SQ SEQUENCE 259 AA; 28861 MW; 2CBFE88F0DD67B61 CRC64;
MTIKIHTEKD FIKMRAAGKL AAETLDFITD HVKPNVTTNS LNDLCHNFIT SHNAIPAPLN
YKGFPKSICT SINHVVCHGI PNDKPLKNGD IVNIDVTVIL DGWYGDTSRM YYVGDVAIKP
KRLIQVTYDA MMKGIEVVRP GAKLGDIGYA IQSYAEKHNY SVVRDYTGHG IGRVFHDKPS
ILNYGRNGTG LTLKEGMFFT VEPMINAGNY DTILSKLDGW TVTTRDKSLS AQFEHTIGVT
KDGFEIFTLS PKKLDYPPY
