O58362 (AMPM_PYRHO) Reviewed, UniProtKB/Swiss-Prot

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:	PH0628

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
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: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal 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 – 295	295	Methionine aminopeptidase		PRO_0000148979
Sites
	Metal binding	82	1	Cobalt 1 By similarity
	Metal binding	93	1	Cobalt 1 By similarity
	Metal binding	93	1	Cobalt 2 By similarity
	Metal binding	153	1	Cobalt 2 By similarity
	Metal binding	187	1	Cobalt 2 By similarity
	Metal binding	280	1	Cobalt 1 By similarity
	Metal binding	280	1	Cobalt 2 By similarity
	Binding site	62	1	Substrate By similarity
	Binding site	161	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O58362 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: D228F4377CEB2AAC	FASTA	295	32,795
	10 20 30 40 50 60 MDVDKLIEAG KIAKKVREEA VKLAKPGVSL LELAEKIESR IVELGGKPAF PANLSLNEVA 70 80 90 100 110 120 AHYTPYKGDQ TVLKEGDYLK IDLGVHIDGY IADTAVTVRV GMDFDELMEA AKEALESAIS 130 140 150 160 170 180 VARAGVEVKE LGKAIENEIR KRGFNPIVNL SGHKIERYKL HAGVSIPNIY RPHDNYVLQE 190 200 210 220 230 240 GDVFAIEPFA TTGAGQVIEV PPTLIYMYVR DAPVRMAQAR FLLAKIKREY KTLPFAYRWL 250 260 270 280 290 QGEMPEGQLK LALRSLERSG ALYGYPVLRE IRGGMVTQFE HTIIVEKDSV TVTTE

References

[1]

"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000001 Genomic DNA. Translation: BAA29717.1.
PIR	C71107.
RefSeq	NP_142587.1. NC_000961.1.
3D structure databases
ProteinModelPortal	O58362.
SMR	O58362. Positions 1-295.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000001553; EBPYRP00000001553; EBPYRG00000001553.
GeneID	1442960.
GenomeReviews	Gene locus PH0628 in contig BA000001_GR.
KEGG	pho:PH0628.
NMPDR	fig|70601.1.peg.613.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000022572.
HOGENOM	HBG318153.
OMA	IEPFATN.
PhylomeDB	O58362.
ProtClustDB	PRK08671.
Enzyme and pathway databases
BioCyc	PHOR70601:PH0628-MONOMER.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002468. Pept_M24A_MAP2. IPR018349. Pept_M24A_MAP2_BS. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 2 hits. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K01265.
PANTHER	PTHR10804:SF9. Pept_M24A_MAP2. 1 hit.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00501. Met_pdase_II. 1 hit.
PROSITE	PS01202. MAP_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM_PYRHO

Accession

Primary (citable) accession number: O58362

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program