Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Methionine aminopeptidase

Gene

map

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 annotation2 Publications

Catalytic activityi

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.UniRule annotation3 Publications

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=2.0 mM for a Met-Gly-Met-Met peptide (for the Fe2+-complexed enzyme)4 Publications
  2. KM=1.3 mM for a Met-Gly-Met-Met peptide (for the Mn2+-complexed enzyme)4 Publications
  3. KM=3.2 mM for a Met-Gly-Met-Met peptide (for the Co2+-complexed enzyme)4 Publications
  1. Vmax=55 µmol/min/mg enzyme (for the Fe2+-complexed enzyme)4 Publications
  2. Vmax=77 µmol/min/mg enzyme (for the Co2+-complexed enzyme)4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei79SubstrateUniRule annotation3 Publications1
Metal bindingi97Divalent metal cation 1UniRule annotation6 Publications1
Binding sitei99Substrate3 Publications1
Metal bindingi108Divalent metal cation 1UniRule annotation6 Publications1
Metal bindingi108Divalent metal cation 2; catalyticUniRule annotation6 Publications1
Metal bindingi171Divalent metal cation 2; catalytic; via tele nitrogenUniRule annotation6 Publications1
Binding sitei178SubstrateUniRule annotation3 Publications1
Metal bindingi204Divalent metal cation 2; catalyticUniRule annotation6 Publications1
Metal bindingi235Divalent metal cation 1UniRule annotation6 Publications1
Metal bindingi235Divalent metal cation 2; catalyticUniRule annotation6 Publications1

GO - Molecular functioni

  • ferrous iron binding Source: EcoCyc
  • metalloaminopeptidase activity Source: EcoCyc

GO - Biological processi

  • protein initiator methionine removal Source: EcoCyc

Keywordsi

Molecular functionAminopeptidase, Hydrolase, Protease
LigandMetal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10570-MONOMER
MetaCyc:EG10570-MONOMER
BRENDAi3.4.11.18 2026
SABIO-RKiP0AE18

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:b0168, JW0163
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10570 map

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi79H → A: Reduces activity 100000-fold for the Co(2+)-complexed enzyme, but only 2.6-fold for the Mn(2+)-complexed enzyme. 2 Publications1
Mutagenesisi97D → A, E or N: Reduces activity 50- to 580-fold depending on the metal ion bound. Binds only one equivalent of the divalent metal cation with affinities identical to the wild-type enzyme. 1 Publication1
Mutagenesisi178H → A: Reduces activity 9000-fold for the Co(2+)-complexed enzyme. Binds only one equivalent of the divalent metal cation with affinities identical to the wild-type enzyme. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL3423
DrugBankiDB08668 3-(5-amino-3-imino-3H-pyrazol-4-ylazo)-benzoic acid
DB08667 4-(4-fluoro-phenylazo)-5-imino-5H-pyrazol-3-ylamine
DB07305 5-(2-CHLORO-4-NITROPHENYL)-2-FUROIC ACID
DB07308 5-(2-CHLOROBENZYL)-2-FUROIC ACID
DB08757 5-(2-chlorophenyl)furan-2-carbohydrazide
DB02909 5-(2-Chlorophenyl)Furan-2-Carboxylic Acid
DB07407 5-(2-METHOXYPHENYL)-2-FUROIC ACID
DB07408 5-(2-NITROPHENYL)-2-FUROIC ACID
DB07304 5-[2-(TRIFLUOROMETHOXY)PHENYL]-2-FUROIC ACID
DB07759 5-[2-(TRIFLUOROMETHYL)PHENYL]-2-FUROIC ACID
DB08671 5-IMINO-4-(2-TRIFLUOROMETHYL-PHENYLAZO)-5H-PYRAZOL-3-YLAMINE
DB08666 5-imino-4-(3-trifluoromethyl-phenylazo)-5H-pyrazol-3-ylamine
DB04015 Methionine Phosphinate
DB02151 Methionine Phosphonate
DB08451 N-(QUINOLIN-8-YL)METHANESULFONAMIDE
DB07591 N1-CYCLOPENTYL-N2-(THIAZOL-2-YL)OXALAMIDE
DB02088 Norleucine Phosphonate
DB03799 Trifluoromethionine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001489372 – 264Methionine aminopeptidaseAdd BLAST263

Proteomic databases

EPDiP0AE18
PaxDbiP0AE18
PRIDEiP0AE18

2D gel databases

SWISS-2DPAGEiP0AE18

Interactioni

Subunit structurei

Monomer.UniRule annotation2 Publications

Protein-protein interaction databases

BioGridi4262194, 76 interactors
DIPiDIP-48040N
IntActiP0AE18, 25 interactors
STRINGi316385.ECDH10B_0147

Chemistry databases

BindingDBiP0AE18

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 28Combined sources21
Helixi29 – 31Combined sources3
Helixi38 – 51Combined sources14
Beta strandi56 – 59Combined sources4
Helixi62 – 64Combined sources3
Beta strandi67 – 73Combined sources7
Beta strandi76 – 78Combined sources3
Beta strandi93 – 102Combined sources10
Beta strandi105 – 114Combined sources10
Beta strandi116 – 118Combined sources3
Helixi120 – 139Combined sources20
Helixi146 – 159Combined sources14
Beta strandi166 – 168Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi174 – 183Combined sources10
Beta strandi200 – 203Combined sources4
Beta strandi206 – 210Combined sources5
Beta strandi214 – 216Combined sources3
Beta strandi218 – 221Combined sources4
Beta strandi223 – 225Combined sources3
Beta strandi231 – 233Combined sources3
Beta strandi235 – 241Combined sources7
Beta strandi244 – 249Combined sources6
Beta strandi258 – 261Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C21X-ray1.80A2-264[»]
1C22X-ray1.75A2-264[»]
1C23X-ray2.00A2-264[»]
1C24X-ray1.70A2-264[»]
1C27X-ray1.95A2-264[»]
1MATX-ray2.40A1-264[»]
1XNZX-ray1.52A1-264[»]
1YVMX-ray1.60A1-264[»]
2BB7X-ray1.70A1-264[»]
2EVCX-ray1.60A1-264[»]
2EVMX-ray1.70A1-264[»]
2EVOX-ray1.70A/B1-264[»]
2GG0X-ray1.28A2-264[»]
2GG2X-ray1.00A2-264[»]
2GG3X-ray1.45A2-264[»]
2GG5X-ray2.12A2-264[»]
2GG7X-ray1.12A2-264[»]
2GG8X-ray1.80A2-264[»]
2GG9X-ray1.05A2-264[»]
2GGBX-ray2.13A2-264[»]
2GGCX-ray1.00A2-264[»]
2GTXX-ray2.00A/B4-264[»]
2GU4X-ray1.80A/B2-264[»]
2GU5X-ray1.60A/B2-264[»]
2GU6X-ray1.70A/B2-264[»]
2GU7X-ray2.00A/B2-264[»]
2MATX-ray1.90A1-264[»]
2P98X-ray1.70A2-262[»]
2P99X-ray1.80A2-262[»]
2P9AX-ray1.60A2-263[»]
2Q92X-ray1.90A2-263[»]
2Q93X-ray1.60A2-264[»]
2Q94X-ray1.63A2-263[»]
2Q95X-ray1.70A2-264[»]
2Q96X-ray1.60A2-264[»]
3D27X-ray2.20A4-264[»]
3MATX-ray2.00A1-264[»]
4MATX-ray2.00A1-264[»]
4Z7MX-ray1.43A/B2-262[»]
ProteinModelPortaliP0AE18
SMRiP0AE18
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AE18

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CA1 Bacteria
COG0024 LUCA
HOGENOMiHOG000030427
InParanoidiP0AE18
KOiK01265
OMAiGDHAYTF
PhylomeDBiP0AE18

Family and domain databases

CDDicd01086 MetAP1, 1 hit
HAMAPiMF_01974 MetAP_1, 1 hit
InterProiView protein in InterPro
IPR036005 Creatinase/aminopeptidase-like
IPR000994 Pept_M24
IPR001714 Pept_M24_MAP
IPR002467 Pept_M24A_MAP1
PfamiView protein in Pfam
PF00557 Peptidase_M24, 1 hit
PRINTSiPR00599 MAPEPTIDASE
SUPFAMiSSF55920 SSF55920, 1 hit
TIGRFAMsiTIGR00500 met_pdase_I, 1 hit
PROSITEiView protein in PROSITE
PS00680 MAP_1, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV
60 70 80 90 100
NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV
110 120 130 140 150
IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG
160 170 180 190 200
AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT
210 220 230 240 250
FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL
260
RKDDTIPAII SHDE
Length:264
Mass (Da):29,331
Last modified:August 1, 1988 - v1
Checksum:iF2D0B57715A67851
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15106 Genomic DNA Translation: AAA24112.1
U70214 Genomic DNA Translation: AAB08597.1
U00096 Genomic DNA Translation: AAC73279.1
AP009048 Genomic DNA Translation: BAB96743.1
PIRiA27761 DPECM
RefSeqiNP_414710.1, NC_000913.3
WP_001018194.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73279; AAC73279; b0168
BAB96743; BAB96743; BAB96743
GeneIDi947882
KEGGiecj:JW0163
eco:b0168
PATRICifig|1411691.4.peg.2113

Similar proteinsi

Entry informationi

Entry nameiMAP1_ECOLI
AccessioniPrimary (citable) accession number: P0AE18
Secondary accession number(s): P07906
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 28, 2018
This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health