Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase B

Gene

slr0786

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: 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 Fe2+-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 sitei102 – 1021SubstrateUniRule annotation
Metal bindingi120 – 1201Divalent metal cation 1UniRule annotation
Metal bindingi131 – 1311Divalent metal cation 1UniRule annotation
Metal bindingi131 – 1311Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi194 – 1941Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei201 – 2011SubstrateUniRule annotation
Metal bindingi227 – 2271Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi258 – 2581Divalent metal cation 1UniRule annotation
Metal bindingi258 – 2581Divalent 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

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1901-MONOMER.

Protein family/group databases

MEROPSiM24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidase BUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAP BUniRule annotation
Short name:
MetAP BUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
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 BPRO_0000148964Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi1148.slr0786.

Structurei

3D structure databases

ProteinModelPortaliP53580.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiP53580.
KOiK01265.
OMAiEGTHEIF.
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

« Hide

        10         20         30         40         50
MNHQNLLSIT RNLVHPPISS GLVLLSAREL DKMRRVGQLA ANLLNHLESM
60 70 80 90 100
VQPGVSTQAL NDEATRWMED HGAISATLGY APPGYPPFTG AICTSINEVV
110 120 130 140 150
CHGIPNPKQI LKDGDIINID VTLRLAGYHG DTSRTFLVGS VSATARKLVE
160 170 180 190 200
ATQESMMRGI AEIKPGARIG DIGAAIQAYA EASGFSVVRD MVGHGIGRQM
210 220 230 240 250
HTELQIPHYG KRGSGLKLRP GMVFTVEPML NEGTYELTFL ADGWTVITKD
260 270
KKLSAQFEHT VVVTEEGVEI LTLA
Length:274
Mass (Da):29,634
Last modified:October 1, 1996 - v1
Checksum:i5DE1A45745A2CB8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
PATRICi23842976. VBISynSp132158_3026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP53580.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi1148.slr0786.

Protein family/group databases

MEROPSiM24.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10691; BAA10691; BAA10691.
GeneIDi952221.
KEGGisyn:slr0786.
PATRICi23842976. VBISynSp132158_3026.

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030427.
InParanoidiP53580.
KOiK01265.
OMAiEGTHEIF.
OrthoDBiEOG6MWNDS.
PhylomeDBiP53580.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-1901-MONOMER.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.