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P69000

- MAP1_CLOAB

UniProt

P69000 - MAP1_CLOAB

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Protein

Methionine aminopeptidase

Gene

map

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.UniRule annotation

Catalytic activityi

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

Cofactori

Co2+UniRule annotation, Zn2+UniRule annotation, Mn2+UniRule annotation, Fe2+UniRule annotationNote: 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 Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei77 – 771SubstrateUniRule annotation
Metal bindingi95 – 951Divalent metal cation 1UniRule annotation
Metal bindingi106 – 1061Divalent metal cation 1UniRule annotation
Metal bindingi106 – 1061Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi169 – 1691Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Metal bindingi202 – 2021Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi233 – 2331Divalent metal cation 1UniRule annotation
Metal bindingi233 – 2331Divalent metal cation 2; catalyticUniRule annotation

GO - Molecular functioni

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

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 aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAPUniRule annotation
Short name:
MetAPUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
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 aminopeptidasePRO_0000148935Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP69000.
SMRiP69000. Positions 1-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

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

        10         20         30         40         50
MIIIKNDTEI EYMRQAGKIV GETLNMLEKA AKPGVTTADL DRLAEDFIKK
60 70 80 90 100
YNAIPSFKGY GGFPASICTS INEEVIHGIP SKHRVLHEGD IISVDCGAIL
110 120 130 140 150
NGYQGDAART FAIGEISEEA AKLIKVTKES FFKGVEKAVI GNRLTDISHS
160 170 180 190 200
IQEYVESFGY GVVRDYVGHG IGKEMHEDPE VPNYGRPGRG PKLVHGMVLA
210 220 230 240 250
IEPMVDVGTY MVKTQSNDWT VVTQDGSLAA HYENTVAILD NGPEILTLCE
Length:250
Mass (Da):27,301
Last modified:February 1, 2005 - v1
Checksum:iFE811B9E55B0584B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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: November 26, 2014
This is version 66 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