P44421 (AMPM_HAEIN) 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:	HI_1722

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	268 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. Binds 1 sodium ion per subunit. The sodium ion has a structural role 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 Reference 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 – 268	268	Methionine aminopeptidase		PRO_0000148940
Sites
	Metal binding	97	1	Cobalt 1 By similarity
	Metal binding	108	1	Cobalt 1 By similarity
	Metal binding	108	1	Cobalt 2 By similarity
	Metal binding	172	1	Cobalt 2 By similarity
	Metal binding	205	1	Cobalt 2 By similarity
	Metal binding	236	1	Cobalt 1 By similarity
	Metal binding	236	1	Cobalt 2 By similarity
	Binding site	79	1	Substrate By similarity
	Binding site	99	1	Substrate By similarity
	Binding site	179	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44421 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: C71DEA15BB5E732B	FASTA	268	29,896
	10 20 30 40 50 60 MAIPIRTEKE IVKLREACKL ASDVLVMIEP YVKAGVTTGE LDRICHEYMV NEQKVIPACL 70 80 90 100 110 120 NYHGFPKATC ISINEVVCHG IPSDDKVLKN GDIVNIDVTV IKDGYFGDNS KMYIVGGETN 130 140 150 160 170 180 IRSKKLVEAA QEALYVGIRT VKPDIRLNEI GKAVQKYTES QTFSVVREYC GHGVGTEFHC 190 200 210 220 230 240 EPQVLHYYAD DGGVILKPGM VFTIEPMINA GKKEVRVMGD GWTVKTKDRS HSAQYEHQLI 250 260 VTETGCEVMT IRDEEIAEGR ISRIMVNV

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23368.1.
PIR	C64138.
RefSeq	NP_439863.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P44421.
SMR	P44421. Positions 2-262.
ModBase	Search...
Protein family/group databases
MEROPS	M24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	950876.
GenomeReviews	Gene locus HI_1722 in contig L42023_GR.
KEGG	hin:HI1722.
NMPDR	fig|71421.1.peg.1634.
PATRIC	20192197. VBIHaeInf48452_1801.
TIGR	HI_1722.
Phylogenomic databases
HOGENOM	HBG299384.
OMA	KKEVRLM.
PhylomeDB	P44421.
ProtClustDB	PRK05716.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1722-MONOMER.
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.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00500. Met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPM_HAEIN

Accession

Primary (citable) accession number: P44421

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program