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P69000

- MAP1_CLOAB

UniProt

P69000 - MAP1_CLOAB

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Protein
Methionine aminopeptidase
Gene
map, CA_C3111
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed By similarity.UniRule annotation

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation

Cofactori

Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe2+-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771Substrate By similarity
Metal bindingi95 – 951Divalent metal cation 1 By similarity
Metal bindingi106 – 1061Divalent metal cation 1 By similarity
Metal bindingi106 – 1061Divalent metal cation 2; catalytic By similarity
Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei176 – 1761Substrate By similarity
Metal bindingi202 – 2021Divalent metal cation 2; catalytic By similarity
Metal bindingi233 – 2331Divalent metal cation 1 By similarity
Metal bindingi233 – 2331Divalent metal cation 2; catalytic By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-HAMAP
  2. metalloaminopeptidase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. protein initiator methionine removal Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase (EC:3.4.11.18)
Short name:
MAP
Short name:
MetAP
Alternative name(s):
Peptidase M
Gene namesi
Name:map
Ordered Locus Names:CA_C3111
OrganismiClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Taxonomic identifieri272562 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000000814: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Methionine aminopeptidaseUniRule annotation
PRO_0000148935Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP69000.
SMRiP69000. Positions 1-248.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

OMAiNYGKPGR.

Family and domain databases

Gene3Di3.90.230.10. 1 hit.
HAMAPiMF_01974. MetAP_1.
InterProiIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
PfamiPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF55920. SSF55920. 1 hit.
TIGRFAMsiTIGR00500. met_pdase_I. 1 hit.
PROSITEiPS00680. MAP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P69000-1 [UniParc]FASTAAdd to Basket

« Hide

MIIIKNDTEI EYMRQAGKIV GETLNMLEKA AKPGVTTADL DRLAEDFIKK    50
YNAIPSFKGY GGFPASICTS INEEVIHGIP SKHRVLHEGD IISVDCGAIL 100
NGYQGDAART FAIGEISEEA AKLIKVTKES FFKGVEKAVI GNRLTDISHS 150
IQEYVESFGY GVVRDYVGHG IGKEMHEDPE VPNYGRPGRG PKLVHGMVLA 200
IEPMVDVGTY MVKTQSNDWT VVTQDGSLAA HYENTVAILD NGPEILTLCE 250
Length:250
Mass (Da):27,301
Last modified:February 1, 2005 - v1
Checksum:iFE811B9E55B0584B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001437 Genomic DNA. No translation available.
RefSeqiYP_008920787.1. NC_003030.1.

Genome annotation databases

GeneIDi1119294.
KEGGicac:CA_C3111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001437 Genomic DNA. No translation available.
RefSeqi YP_008920787.1. NC_003030.1.

3D structure databases

ProteinModelPortali P69000.
SMRi P69000. Positions 1-248.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 1119294.
KEGGi cac:CA_C3111.

Phylogenomic databases

OMAi NYGKPGR.

Family and domain databases

Gene3Di 3.90.230.10. 1 hit.
HAMAPi MF_01974. MetAP_1.
InterProi IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view ]
Pfami PF00557. Peptidase_M24. 1 hit.
[Graphical view ]
PRINTSi PR00599. MAPEPTIDASE.
SUPFAMi SSF55920. SSF55920. 1 hit.
TIGRFAMsi TIGR00500. met_pdase_I. 1 hit.
PROSITEi PS00680. MAP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
  2. "Improving genome annotations using phylogenetic profile anomaly detection."
    Mikkelsen T.S., Galagan J.E., Mesirov J.P.
    Bioinformatics 21:464-470(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiMAP1_CLOAB
AccessioniPrimary (citable) accession number: P69000
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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