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P44421

- MAP1_HAEIN

UniProt

P44421 - MAP1_HAEIN

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Protein

Methionine aminopeptidase

Gene

map

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
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.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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791SubstrateUniRule annotation
Metal bindingi97 – 971Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 1UniRule annotation
Metal bindingi108 – 1081Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi172 – 1721Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation
Binding sitei179 – 1791SubstrateUniRule annotation
Metal bindingi205 – 2051Divalent metal cation 2; catalyticUniRule annotation
Metal bindingi236 – 2361Divalent metal cation 1UniRule annotation
Metal bindingi236 – 2361Divalent metal cation 2; catalyticUniRule annotation

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

Protein family/group databases

MEROPSiM24.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionine aminopeptidaseUniRule annotation (EC:3.4.11.18UniRule annotation)
Short name:
MAPUniRule annotation
Short name:
MetAPUniRule annotation
Alternative name(s):
Peptidase MUniRule annotation
Gene namesi
Name:mapUniRule annotation
Ordered Locus Names:HI_1722
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 268268Methionine aminopeptidasePRO_0000148940Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi71421.HI1722.

Structurei

3D structure databases

ProteinModelPortaliP44421.
SMRiP44421. Positions 2-262.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0024.
KOiK01265.
OMAiEGMCFTI.
OrthoDBiEOG6MWNDS.
PhylomeDBiP44421.

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.

P44421-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAIPIRTEKE IVKLREACKL ASDVLVMIEP YVKAGVTTGE LDRICHEYMV
60 70 80 90 100
NEQKVIPACL NYHGFPKATC ISINEVVCHG IPSDDKVLKN GDIVNIDVTV
110 120 130 140 150
IKDGYFGDNS KMYIVGGETN IRSKKLVEAA QEALYVGIRT VKPDIRLNEI
160 170 180 190 200
GKAVQKYTES QTFSVVREYC GHGVGTEFHC EPQVLHYYAD DGGVILKPGM
210 220 230 240 250
VFTIEPMINA GKKEVRVMGD GWTVKTKDRS HSAQYEHQLI VTETGCEVMT
260
IRDEEIAEGR ISRIMVNV
Length:268
Mass (Da):29,896
Last modified:November 1, 1995 - v1
Checksum:iC71DEA15BB5E732B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC23368.1.
PIRiC64138.
RefSeqiNP_439863.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC23368; AAC23368; HI_1722.
GeneIDi950876.
KEGGihin:HI1722.
PATRICi20192197. VBIHaeInf48452_1801.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC23368.1 .
PIRi C64138.
RefSeqi NP_439863.1. NC_000907.1.

3D structure databases

ProteinModelPortali P44421.
SMRi P44421. Positions 2-262.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI1722.

Protein family/group databases

MEROPSi M24.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC23368 ; AAC23368 ; HI_1722 .
GeneIDi 950876.
KEGGi hin:HI1722.
PATRICi 20192197. VBIHaeInf48452_1801.

Phylogenomic databases

eggNOGi COG0024.
KOi K01265.
OMAi EGMCFTI.
OrthoDBi EOG6MWNDS.
PhylomeDBi P44421.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Entry informationi

Entry nameiMAP1_HAEIN
AccessioniPrimary (citable) accession number: P44421
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 1, 2014
This is version 105 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, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3