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P53580

- MAP12_SYNY3

UniProt

P53580 - MAP12_SYNY3

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Protein
Methionine aminopeptidase B
Gene
slr0786
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
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 sitei102 – 1021Substrate By similarity
Metal bindingi120 – 1201Divalent metal cation 1 By similarity
Metal bindingi131 – 1311Divalent metal cation 1 By similarity
Metal bindingi131 – 1311Divalent metal cation 2; catalytic By similarity
Metal bindingi194 – 1941Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei201 – 2011Substrate By similarity
Metal bindingi227 – 2271Divalent metal cation 2; catalytic By similarity
Metal bindingi258 – 2581Divalent metal cation 1 By similarity
Metal bindingi258 – 2581Divalent 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

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1901-MONOMER.

Protein family/group databases

MEROPSiM24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase B (EC:3.4.11.18)
Short name:
MAP B
Short name:
MetAP B
Alternative name(s):
Peptidase M
Gene namesi
Ordered Locus Names:slr0786
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
ProteomesiUP000001425: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Methionine aminopeptidase BUniRule annotation
PRO_0000148964Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi1148.slr0786.

Structurei

3D structure databases

ProteinModelPortaliP53580.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
KOiK01265.
OMAiHLCESAN.
OrthoDBiEOG6MWNDS.
PhylomeDBiP53580.

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.

P53580-1 [UniParc]FASTAAdd to Basket

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MNHQNLLSIT RNLVHPPISS GLVLLSAREL DKMRRVGQLA ANLLNHLESM    50
VQPGVSTQAL NDEATRWMED HGAISATLGY APPGYPPFTG AICTSINEVV 100
CHGIPNPKQI LKDGDIINID VTLRLAGYHG DTSRTFLVGS VSATARKLVE 150
ATQESMMRGI AEIKPGARIG DIGAAIQAYA EASGFSVVRD MVGHGIGRQM 200
HTELQIPHYG KRGSGLKLRP GMVFTVEPML NEGTYELTFL ADGWTVITKD 250
KKLSAQFEHT VVVTEEGVEI LTLA 274
Length:274
Mass (Da):29,634
Last modified:October 1, 1996 - v1
Checksum:i5DE1A45745A2CB8E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000022 Genomic DNA. Translation: BAA10691.1.
PIRiS76999.
RefSeqiNP_442620.1. NC_000911.1.
YP_005652681.1. NC_017277.1.
YP_007452496.1. NC_020286.1.

Genome annotation databases

EnsemblBacteriaiBAA10691; BAA10691; BAA10691.
GeneIDi952221.
KEGGisyn:slr0786.
syy:SYNGTS_2728.
syz:MYO_127540.
PATRICi23842976. VBISynSp132158_3026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000022 Genomic DNA. Translation: BAA10691.1 .
PIRi S76999.
RefSeqi NP_442620.1. NC_000911.1.
YP_005652681.1. NC_017277.1.
YP_007452496.1. NC_020286.1.

3D structure databases

ProteinModelPortali P53580.
ModBasei Search...

Protein-protein interaction databases

STRINGi 1148.slr0786.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA10691 ; BAA10691 ; BAA10691 .
GeneIDi 952221.
KEGGi syn:slr0786.
syy:SYNGTS_2728.
syz:MYO_127540.
PATRICi 23842976. VBISynSp132158_3026.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030427.
KOi K01265.
OMAi HLCESAN.
OrthoDBi EOG6MWNDS.
PhylomeDBi P53580.

Enzyme and pathway databases

BioCyci RETL1328306-WGS:GSTH-1901-MONOMER.

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

  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
    Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
    DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27184 / PCC 6803 / N-1.
  2. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.

Entry informationi

Entry nameiMAP12_SYNY3
AccessioniPrimary (citable) accession number: P53580
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 102 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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

External Data

Dasty 3

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