V5VCW7 · V5VCW7_ACIBA

  • Protein
    Methionine aminopeptidase
  • Gene
    map
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

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.

Catalytic activity

  • Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
    EC:3.4.11.18 (UniProtKB | ENZYME | Rhea)

Cofactor

Co2+ (UniProtKB | Rhea| CHEBI:48828 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Fe2+ (UniProtKB | Rhea| CHEBI:29033 )

Note: 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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site92substrate
Binding site110a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site121a divalent metal cation 1 (UniProtKB | ChEBI)
Binding site121a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site185a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site192substrate
Binding site218a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site249a divalent metal cation 2 (UniProtKB | ChEBI); catalytic
Binding site249a divalent metal cation 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functioninitiator methionyl aminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloaminopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Methionine aminopeptidase
  • EC number
  • Short names
    MAP
    ; MetAP
  • Alternative names
    • Peptidase M

Gene names

    • Name
      map
    • Synonyms
      map1
      , map3
      , map_1
      , map_2
    • ORF names
      A6Y97_09645
      , A7M90_04815
      , ABR2091_2512
      , ABUW_1234
      , APD33_02645
      , APD33_12805
      , AUO97_00550
      , B9W25_05720
      , B9X95_11705
      , CBE85_00465
      , CV954_005965
      , CV955_0006050
      , DOL94_04640
      , EA706_00955
      , EA722_08630
      , EKS29_06595
      , EWP49_05205
      , F2P40_02010
      , F4T85_00585
      , FJU36_01850
      , FJU42_15260
      , FPK81_01780
      , FQZ15_06245
      , FR761_12845
      , G3N53_09925
      , GNY86_13630
      , GSE42_14095
      , H0529_01220
      , IAG11_02480
      , IHV20_12435
      , IMO23_12425
      , J6E47_06120
      , LV35_03405
      , MKP18_000955
      , NCTC13305_03581
      , OMP06_13210
      , P9867_17035
      , SAMEA104305318_02021
      , SAMEA104305340_01940
      , SAMEA4394745_01927

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • ATCC 17978
    • ATCC 17978-VU
    • AB5075-UW
    • ABBL072
    • R2091
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter > Acinetobacter calcoaceticus/baumannii complex

Accessions

  • Primary accession
    V5VCW7

Proteomes

Subcellular Location

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain19-256Peptidase M24

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    275
  • Mass (Da)
    30,374
  • Last updated
    2014-02-19 v1
  • Checksum
    6D82AB2AE6DC1802
MNSTYTAPRRLIKTPDEIEKMRIAGRLAAEVLDMIKPHIKAGVSTLELDTICRNHIENVQHAIPACVGYGGAPGRPAFQHSICTSVNHVVCHGIPSENKILKNGDILNIDVTVIKDGYHGDTNMMYIVGGETSILANRLCKVAQEAMYRGMATVRDGSYLGDIGHAIQKYVESERFSVVREYCGHGIGTVFHDEPQVLHYGQAGTGMRLEAGMTFTIEPMVNAGVWQTKLLGDKWTVVTKDHKLSAQYEHTILVTKTGIEVLTARPEEDLSRFNQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP008706
EMBL· GenBank· DDBJ
AKA30982.1
EMBL· GenBank· DDBJ
Genomic DNA
CP018664
EMBL· GenBank· DDBJ
APP29388.1
EMBL· GenBank· DDBJ
Genomic DNA
LN997846
EMBL· GenBank· DDBJ
CUW35909.1
EMBL· GenBank· DDBJ
Genomic DNA
ABFEVW020000005
EMBL· GenBank· DDBJ
EKU3567577.1
EMBL· GenBank· DDBJ
Genomic DNA
ABFEVW030000005
EMBL· GenBank· DDBJ
EMN1070674.1
EMBL· GenBank· DDBJ
Genomic DNA
VYVC01000012
EMBL· GenBank· DDBJ
KAA9221432.1
EMBL· GenBank· DDBJ
Genomic DNA
LLGC01000179
EMBL· GenBank· DDBJ
KQE03489.1
EMBL· GenBank· DDBJ
Genomic DNA
LLGC01000126
EMBL· GenBank· DDBJ
KQE07355.1
EMBL· GenBank· DDBJ
Genomic DNA
LRDT01000044
EMBL· GenBank· DDBJ
KZA12740.1
EMBL· GenBank· DDBJ
Genomic DNA
JACSVK010000003
EMBL· GenBank· DDBJ
MBD0218758.1
EMBL· GenBank· DDBJ
Genomic DNA
JACZEI010000027
EMBL· GenBank· DDBJ
MBE0330955.1
EMBL· GenBank· DDBJ
Genomic DNA
JARTMM010000087
EMBL· GenBank· DDBJ
MDK4883330.1
EMBL· GenBank· DDBJ
Genomic DNA
VMAW01000001
EMBL· GenBank· DDBJ
MDT1909774.1
EMBL· GenBank· DDBJ
Genomic DNA
WIOC01000002
EMBL· GenBank· DDBJ
MQR48113.1
EMBL· GenBank· DDBJ
Genomic DNA
VYTH01000001
EMBL· GenBank· DDBJ
MQZ66891.1
EMBL· GenBank· DDBJ
Genomic DNA
WPIP01000105
EMBL· GenBank· DDBJ
MVM92566.1
EMBL· GenBank· DDBJ
Genomic DNA
WWCH01000001
EMBL· GenBank· DDBJ
MYM79056.1
EMBL· GenBank· DDBJ
Genomic DNA
JAAGTY010000009
EMBL· GenBank· DDBJ
NDW41392.1
EMBL· GenBank· DDBJ
Genomic DNA
LYKI01000023
EMBL· GenBank· DDBJ
OIG72371.1
EMBL· GenBank· DDBJ
Genomic DNA
NGEL01000129
EMBL· GenBank· DDBJ
OTM85450.1
EMBL· GenBank· DDBJ
Genomic DNA
NGKM01000001
EMBL· GenBank· DDBJ
OWK68248.1
EMBL· GenBank· DDBJ
Genomic DNA
PHJU02000014
EMBL· GenBank· DDBJ
PQL84274.1
EMBL· GenBank· DDBJ
Genomic DNA
PHJT03000020
EMBL· GenBank· DDBJ
PQL88375.1
EMBL· GenBank· DDBJ
Genomic DNA
NEPB01000008
EMBL· GenBank· DDBJ
PRN35987.1
EMBL· GenBank· DDBJ
Genomic DNA
QKWF01000036
EMBL· GenBank· DDBJ
PZM18289.1
EMBL· GenBank· DDBJ
Genomic DNA
CP042556
EMBL· GenBank· DDBJ
QFH46123.1
EMBL· GenBank· DDBJ
Genomic DNA
CP061521
EMBL· GenBank· DDBJ
QNV30414.1
EMBL· GenBank· DDBJ
Genomic DNA
CP059300
EMBL· GenBank· DDBJ
QOJ60316.1
EMBL· GenBank· DDBJ
Genomic DNA
CP062919
EMBL· GenBank· DDBJ
QPF12406.1
EMBL· GenBank· DDBJ
Genomic DNA
CP072270
EMBL· GenBank· DDBJ
QTK44638.1
EMBL· GenBank· DDBJ
Genomic DNA
RFBY01000023
EMBL· GenBank· DDBJ
RSP76616.1
EMBL· GenBank· DDBJ
Genomic DNA
RFCO01000002
EMBL· GenBank· DDBJ
RSQ49839.1
EMBL· GenBank· DDBJ
Genomic DNA
RXYO01000031
EMBL· GenBank· DDBJ
RTY10994.1
EMBL· GenBank· DDBJ
Genomic DNA
SEUG01000001
EMBL· GenBank· DDBJ
RYL46242.1
EMBL· GenBank· DDBJ
Genomic DNA
UFDJ01000008
EMBL· GenBank· DDBJ
SSI43005.1
EMBL· GenBank· DDBJ
Genomic DNA
UFMQ01000008
EMBL· GenBank· DDBJ
SST23566.1
EMBL· GenBank· DDBJ
Genomic DNA
UFNM01000007
EMBL· GenBank· DDBJ
SSU08101.1
EMBL· GenBank· DDBJ
Genomic DNA
UFSC01000003
EMBL· GenBank· DDBJ
SUU32078.1
EMBL· GenBank· DDBJ
Genomic DNA
VHGY01000042
EMBL· GenBank· DDBJ
TPU61657.1
EMBL· GenBank· DDBJ
Genomic DNA
VHGX01000005
EMBL· GenBank· DDBJ
TPU81270.1
EMBL· GenBank· DDBJ
Genomic DNA
CP110462
EMBL· GenBank· DDBJ
UZG61185.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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