(data stored in ACNUC7421 zone)

SWISSPROT: C1ARM0_RHOOB

ID   C1ARM0_RHOOB            Unreviewed;       261 AA.
AC   C1ARM0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE            Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN   Name=map {ECO:0000256|HAMAP-Rule:MF_01974,
GN   ECO:0000313|EMBL:BAH48697.1};
GN   OrderedLocusNames=ROP_04500 {ECO:0000313|EMBL:BAH48697.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48697.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48697.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48697.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC       {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC       Note=Binds 2 divalent metal cations per subunit. Has a high-
CC       affinity and a low affinity metal-binding site. The true nature of
CC       the physiological cofactor is under debate. The enzyme is active
CC       with cobalt, zinc, manganese or divalent iron ions. Most likely,
CC       methionine aminopeptidases function as mononuclear Fe(2+)-
CC       metalloproteases under physiological conditions, and the
CC       catalytically relevant metal-binding site has been assigned to the
CC       histidine-containing high-affinity site. {ECO:0000256|HAMAP-
CC       Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP011115; BAH48697.1; -; Genomic_DNA.
DR   ProteinModelPortal; C1ARM0; -.
DR   STRING; 632772.ROP_04500; -.
DR   EnsemblBacteria; BAH48697; BAH48697; ROP_04500.
DR   KEGG; rop:ROP_04500; -.
DR   PATRIC; fig|632772.20.peg.501; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   HOGENOM; HOG000030426; -.
DR   KO; K01265; -.
DR   OMA; SYFHGPP; -.
DR   OrthoDB; POG091H01DX; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP.
DR   CDD; cd01086; MetAP1; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
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   3: Inferred from homology;
DR   PRODOM; C1ARM0.
DR   SWISS-2DPAGE; C1ARM0.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:BAH48697.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000313|EMBL:BAH48697.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653}.
FT   DOMAIN       16    250       Peptidase_M24. {ECO:0000259|Pfam:
FT                                PF00557}.
FT   METAL       105    105       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       116    116       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       116    116       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       179    179       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   METAL       212    212       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       243    243       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       243    243       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   BINDING      88     88       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
SQ   SEQUENCE   261 AA;  28288 MW;  F90BA35F3F490B53 CRC64;
     MEDERVLELK TPREIEAMRT TGAFIAELLD DLQSRAAVGV NLLDLEHRAR HLIKDRGAVS
     CYWDYAPSFG RGPFHNVICL SVNDAVLHGL PHDYTLRDGD LLSMDIAVSI DGWVADSARS
     LIVGTPHAGD QRLIEATERA LDAGIDAARP GRRLGDISAA IGAVATDYGF PVNTEFGGHG
     LGRTMHEDPH VSNQGRAGRG LVLRPGLTLA LEPWFARGTD KIVYDPDGWT IRSADGSRTA
     HSEHTIAITD GDPLVLTRRS A
//

If you have problems or comments...

PBIL Back to PBIL home page