Reviewed, UniProtKB/Swiss-Prot Q11132 (AMPM_MYCPN)

Names and origin

Protein names

Recommended name:
    Methionine aminopeptidase
      Short name=MAP
    EC=3.4.11.18
Alternative name(s):
    Peptidase M

Gene names

Name:	map
Ordered Locus Names:	MPN_186
ORF Names:	MP645

Organism

Mycoplasma pneumoniae [Complete proteome] [HAMAP]

Taxonomic identifier

2104 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity.
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.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 248	248	Methionine aminopeptidase		PRO_0000148947
Sites
	Metal binding	94	1	Cobalt 1 By similarity
	Metal binding	105	1	Cobalt 1 By similarity
	Metal binding	105	1	Cobalt 2 By similarity
	Metal binding	169	1	Cobalt 2 By similarity
	Metal binding	202	1	Cobalt 2 By similarity
	Metal binding	233	1	Cobalt 1 By similarity
	Metal binding	233	1	Cobalt 2 By similarity
	Binding site	77	1	Substrate By similarity
	Binding site	176	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q11132-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: D3F4B5F3F6048BF5	FASTA	248	27,657
	10 20 30 40 50 60 MVYLKSAREV EQIRQACKIF QEAKAYFTIE RLLGKSLTAI DQALKQFIES KGATCAFHKY 70 80 90 100 110 120 QNFPGFNCLS LNETVIHGIA DNRVFGVKDK LTLDIGINLN GYICDAAFTV LGPKAPEPMQ 130 140 150 160 170 180 TLLEVTEACF TAVVEPQLRP NNPTGNVSHA IQTYFESKGY YLLKQFGGHG CGIKVHEEPL 190 200 210 220 230 240 ILNYGKPDTG TKLEPGMVLC IEPMVMTDSD AMVMHNNSWN VLTPKSRYNC HVEQMYVITT SGFECLTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma pneumoniae comprising the dnaA region, the atp operon and a cluster of ribosomal protein genes." Hilbert H., Himmelreich R., Plagens H., Herrmann R. Nucleic Acids Res. 24:628-639(1996) [PubMed: 8604303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29342 / M129.
[2]	"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae." Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R. Nucleic Acids Res. 24:4420-4449(1996) [PubMed: 8948633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29342 / M129.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U34795 Genomic DNA. Translation: AAC43695.1. U00089 Genomic DNA. Translation: AAB96293.1.
PIR	S62822.
RefSeq	NP_109874.1.
3D structure databases
HSSP	HSSP built from PDB template 1O0X based on UniProtKB Q9X1I7.
ModBase	Search...
Genome annotation databases
GeneID	876883.
GenomeReviews	Gene locus MPN_186 in contig U00089_GR.
KEGG	mpn:MPN186.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q11132.
OMA	PVNTEFG.
Enzyme and pathway databases
BioCyc	MPNE272634:MPN186-MON.
BRENDA	3.4.11.18. 39500.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
PANTHER	PTHR10804:SF13. Pept_M24A_MAP1. 1 hit. PTHR10804. Peptidase_M24_cat_core. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
TIGRFAMs	TIGR00500. met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM_MYCPN

Accession

Primary (citable) accession number: Q11132

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)