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Reviewed, UniProtKB/Swiss-Prot Q9Z9J4 (AMPM_BACHD)

Last modified November 3, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Methionine aminopeptidase
      Short name=MAP
    EC=3.4.11.18
Alternative name(s):
    Peptidase M
Gene names
Name: map
Ordered Locus Names: BH0156
OrganismBacillus halodurans [Complete proteome] [HAMAP]
Taxonomic identifier86665 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Removes the amino-terminal methionine from nascent proteins.

Catalytic activity

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

Cofactor

Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.

Sequence similarities

Belongs to the peptidase M24A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 248248Methionine aminopeptidase
PRO_0000148925

Sites

Metal binding941Cobalt 1 By similarity
Metal binding1051Cobalt 1 By similarity
Metal binding1051Cobalt 2 By similarity
Metal binding1681Cobalt 2 By similarity
Metal binding2011Cobalt 2 By similarity
Metal binding2321Cobalt 1 By similarity
Metal binding2321Cobalt 2 By similarity
Binding site771Substrate By similarity
Binding site1751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z9J4-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C2295A5147447327

FASTA24827,155
        10         20         30         40         50         60 
MIICKTEREL EIMREAGRIV ALTHQEIKLH IQPGITTKKL DEIAETFIRS HGATPSFKGY 

        70         80         90        100        110        120 
NGFTGSICAS VNEELVHGIP GNRVLKEGDI ISVDIGAKYN GYHGDSAWTY AVGNISDEDQ 

       130        140        150        160        170        180 
DLLDVTETSL YKGLEQAKAG ARLSDISHAI QSYAEPRGYA IVREYVGHGV GQNLHEDPQI 

       190        200        210        220        230        240 
PHYGPPGKGP RLKPGMVLAI EPMVNAGSRY VRTLSDNWTV VTVDGKKCAH FEHTIAITET 


GYEILTKA 

« Hide

References

« Hide 'large scale' references
[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: 10192928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.
[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: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153.

Cross-references

Sequence databases

AB017508 Genomic DNA. Translation: BAA75293.1.
BA000004 Genomic DNA. Translation: BAB03875.1.
PIRT44405.
RefSeqNP_241022.1.

3D structure databases

HSSPHSSP built from PDB template 1O0X based on UniProtKB Q9X1I7.
ModBaseSearch...

Protein family/group databases

MEROPSM24.001.

Genome annotation databases

GeneID893603.
GenomeReviewsGene locus BH0156 in contig BA000004_GR.
KEGGbha:BH0156.
NMPDRfig|272558.1.peg.156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9Z9J4.
OMATATGPRI.

Enzyme and pathway databases

BioCycBHAL272558:BH0156-MON.
BRENDA3.4.11.18. 191865.

Family and domain databases

InterProIPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR002467. Pept_M24A_MAP1.
[Graphical view]
Gene3DG3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHERPTHR10804:SF13. Pept_M24A_MAP1. 1 hit.
PTHR10804. Peptidase_M24_cat_core. 1 hit.
PfamPF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSPR00599. MAPEPTIDASE.
TIGRFAMsTIGR00500. met_pdase_I. 1 hit.
PROSITEPS00680. MAP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPM_BACHD
AccessionPrimary (citable) accession number: Q9Z9J4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents