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O52353

- MAP1_MYCGA

UniProt

O52353 - MAP1_MYCGA

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Protein

Methionine aminopeptidase

Gene

map

Organism
Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
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

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 sitei77 – 771SubstrateUniRule annotation
Metal bindingi94 – 941Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent metal cation 1UniRule annotation
Metal bindingi105 – 1051Divalent 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 bindingi235 – 2351Divalent metal cation 1UniRule annotation
Metal bindingi235 – 2351Divalent 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

BioCyciMGAL710127:GC09-73-MONOMER.

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:MYCGA0720
ORF Names:MGA_0745
OrganismiMycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
Taxonomic identifieri710127 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000001418: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Methionine aminopeptidasePRO_0000148945Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi233150.MGA_0745.

Structurei

3D structure databases

ProteinModelPortaliO52353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0024.
HOGENOMiHOG000030426.
KOiK01265.
OMAiNIIQTHA.
OrthoDBiEOG6MWNDS.

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.

O52353-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIYIKNPNEI QKIKNAAQIY KKIVKQFNFD YIKNKSLKEI DQMLRDFVSQ
60 70 80 90 100
HHANSCYHGY LGFKGYHCLS LNQTIIHGLA NDEIFTSKDK LTIDIGIELD
110 120 130 140 150
NYYCDSAFTI LGPDVNPRQK LLSEVTHNCI FELVKKIVPN QTTTNDLGIW
160 170 180 190 200
TEEYAKKYGY SVIKDFGGHG CGIKIHEDPI ILNYGTKKSS ELLTPNMVIC
210 220 230 240 250
IEPMFFEKDN RYYIDPDDSW SVKPVNKNQY VCHWEHMVLI KEDQAEILTL
Length:250
Mass (Da):29,026
Last modified:August 15, 2003 - v2
Checksum:iF7EE9B91D4779F76
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731Q → K in AAB95408. (PubMed:10867916)Curated
Sequence conflicti83 – 831E → D in AAB95408. (PubMed:10867916)Curated
Sequence conflicti117 – 1171P → L in AAB95408. (PubMed:10867916)Curated
Sequence conflicti132 – 1321E → D in AAB95408. (PubMed:10867916)Curated
Sequence conflicti158 – 1581Y → H in AAB95408. (PubMed:10867916)Curated
Sequence conflicti161 – 1611S → N in AAB95408. (PubMed:10867916)Curated
Sequence conflicti189 – 1902SS → PG in AAB95408. (PubMed:10867916)Curated
Sequence conflicti217 – 2171D → V in AAB95408. (PubMed:10867916)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF036708 Genomic DNA. Translation: AAB95408.1.
AE015450 Genomic DNA. Translation: AAP56422.1.
RefSeqiNP_852854.1. NC_004829.2.
WP_011113301.1. NC_004829.2.

Genome annotation databases

EnsemblBacteriaiAAP56422; AAP56422; MGA_0745.
GeneIDi1090121.
KEGGimga:MGA_0745.
PATRICi20007816. VBIMycGal115357_0076.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF036708 Genomic DNA. Translation: AAB95408.1 .
AE015450 Genomic DNA. Translation: AAP56422.1 .
RefSeqi NP_852854.1. NC_004829.2.
WP_011113301.1. NC_004829.2.

3D structure databases

ProteinModelPortali O52353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 233150.MGA_0745.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP56422 ; AAP56422 ; MGA_0745 .
GeneIDi 1090121.
KEGGi mga:MGA_0745.
PATRICi 20007816. VBIMycGal115357_0076.

Phylogenomic databases

eggNOGi COG0024.
HOGENOMi HOG000030426.
KOi K01265.
OMAi NIIQTHA.
OrthoDBi EOG6MWNDS.

Enzyme and pathway databases

BioCyci MGAL710127:GC09-73-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

« Hide 'large scale' publications
  1. "Determination and analysis of the nucleotide sequence of a segment of a Mycoplasma gallisepticum strain A5969 chromosome, containing operons S10 and rrn23-5."
    Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.
    Mol. Biol. (Mosk.) 34:390-396(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A5969Var.B.
  2. "The complete genome sequence of the avian pathogen Mycoplasma gallisepticum strain R(low)."
    Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F., Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.
    Microbiology 149:2307-2316(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: R(low / passage 15 / clone 2).

Entry informationi

Entry nameiMAP1_MYCGA
AccessioniPrimary (citable) accession number: O52353
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 15, 2003
Last modified: October 29, 2014
This is version 108 of the entry and version 2 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