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Q9Z9J4

- MAP1_BACHD

UniProt

Q9Z9J4 - MAP1_BACHD

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Protein

Methionine aminopeptidase

Gene
map, BH0156
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
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 bindingi94 – 941Divalent metal cation 1 By similarity
Metal bindingi105 – 1051Divalent metal cation 1 By similarity
Metal bindingi105 – 1051Divalent metal cation 2; catalytic By similarity
Metal bindingi168 – 1681Divalent metal cation 2; catalytic; via tele nitrogen By similarity
Binding sitei175 – 1751Substrate By similarity
Metal bindingi201 – 2011Divalent metal cation 2; catalytic By similarity
Metal bindingi232 – 2321Divalent metal cation 1 By similarity
Metal bindingi232 – 2321Divalent metal cation 2; catalytic By similarity

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

BioCyciBHAL272558:GJC5-181-MONOMER.

Protein family/group databases

MEROPSiM24.001.

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:BH0156
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248Methionine aminopeptidaseUniRule annotationPRO_0000148925Add
BLAST

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272558.BH0156.

Structurei

3D structure databases

ProteinModelPortaliQ9Z9J4.
SMRiQ9Z9J4. Positions 1-248.

Family & Domainsi

Sequence similaritiesi

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.

Q9Z9J4-1 [UniParc]FASTAAdd to Basket

« Hide

MIICKTEREL EIMREAGRIV ALTHQEIKLH IQPGITTKKL DEIAETFIRS    50
HGATPSFKGY NGFTGSICAS VNEELVHGIP GNRVLKEGDI ISVDIGAKYN 100
GYHGDSAWTY AVGNISDEDQ DLLDVTETSL YKGLEQAKAG ARLSDISHAI 150
QSYAEPRGYA IVREYVGHGV GQNLHEDPQI PHYGPPGKGP RLKPGMVLAI 200
EPMVNAGSRY VRTLSDNWTV VTVDGKKCAH FEHTIAITET GYEILTKA 248
Length:248
Mass (Da):27,155
Last modified:May 1, 1999 - v1
Checksum:iC2295A5147447327
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017508 Genomic DNA. Translation: BAA75293.1.
BA000004 Genomic DNA. Translation: BAB03875.1.
PIRiT44405.
RefSeqiNP_241022.1. NC_002570.2.
WP_010896339.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB03875; BAB03875; BAB03875.
GeneIDi893603.
KEGGibha:BH0156.
PATRICi18937186. VBIBacHal18977_0165.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017508 Genomic DNA. Translation: BAA75293.1 .
BA000004 Genomic DNA. Translation: BAB03875.1 .
PIRi T44405.
RefSeqi NP_241022.1. NC_002570.2.
WP_010896339.1. NC_002570.2.

3D structure databases

ProteinModelPortali Q9Z9J4.
SMRi Q9Z9J4. Positions 1-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272558.BH0156.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB03875 ; BAB03875 ; BAB03875 .
GeneIDi 893603.
KEGGi bha:BH0156.
PATRICi 18937186. VBIBacHal18977_0165.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BHAL272558:GJC5-181-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. "Sequence analysis of a 32-kb region including the major ribosomal protein gene clusters from alkaliphilic Bacillus sp. strain C-125."
    Takami H., Takaki Y., Nakasone K., Hirama C., Inoue A., Horikoshi K.
    Biosci. Biotechnol. Biochem. 63:452-455(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
  2. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Entry informationi

Entry nameiMAP1_BACHD
AccessioniPrimary (citable) accession number: Q9Z9J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 104 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

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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