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ECOLI:AMPM

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) map
Protein Name(s) Methionine aminopeptidase

MAP Peptidase M

External Links
UniProt P0AE18
EMBL M15106
U70214
U00096
AP009048
PIR A27761
RefSeq NP_414710.1
YP_488470.1
PDB 1C21
1C22
1C23
1C24
1C27
1MAT
1XNZ
1YVM
2BB7
2EVC
2EVM
2EVO
2GG0
2GG2
2GG3
2GG5
2GG7
2GG8
2GG9
2GGB
2GGC
2GTX
2GU4
2GU5
2GU6
2GU7
2MAT
2P98
2P99
2P9A
2Q92
2Q93
2Q94
2Q95
2Q96
3D27
3MAT
4MAT
PDBsum 1C21
1C22
1C23
1C24
1C27
1MAT
1XNZ
1YVM
2BB7
2EVC
2EVM
2EVO
2GG0
2GG2
2GG3
2GG5
2GG7
2GG8
2GG9
2GGB
2GGC
2GTX
2GU4
2GU5
2GU6
2GU7
2MAT
2P98
2P99
2P9A
2Q92
2Q93
2Q94
2Q95
2Q96
3D27
3MAT
4MAT
ProteinModelPortal P0AE18
SMR P0AE18
DIP DIP-48040N
IntAct P0AE18
MINT MINT-1219572
STRING 511145.b0168
MEROPS M24.001
SWISS-2DPAGE P0AE18
PaxDb P0AE18
PRIDE P0AE18
EnsemblBacteria AAC73279
BAB96743
GeneID 12933200
947882
KEGG ecj:Y75_p0164
eco:b0168
PATRIC 32115443
EchoBASE EB0565
EcoGene EG10570
eggNOG COG0024
HOGENOM HOG000030427
KO K01265
OMA GEVIQKH
ProtClustDB PRK05716
BioCyc EcoCyc:EG10570-MONOMER
ECOL316407:JW0163-MONOMER
MetaCyc:EG10570-MONOMER
SABIO-RK P0AE18
BindingDB P0AE18
ChEMBL CHEMBL3423
EvolutionaryTrace P0AE18
Genevestigator P0AE18
GO GO:0005829
GO:0008198
GO:0070006
GO:0070084
GO:0006508
Gene3D 3.90.230.10
InterPro IPR001714
IPR000994
IPR002467
Pfam PF00557
PRINTS PR00599
SUPFAM SSF55920
TIGRFAMs TIGR00500
PROSITE PS00680

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0070084

protein initiator methionine removal

PMID:3027045[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0070006

metalloaminopeptidase activity

PMID:3027045[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008198

ferrous iron binding

PMID:18669631[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17272300[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004177

aminopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002467

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002467

P

Seeded From UniProt

complete

enables

GO:0008235

metalloexopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002467

F

Seeded From UniProt

complete

involved_in

GO:0070084

protein initiator methionine removal

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000161491

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000161491

F

Seeded From UniProt

complete

enables

GO:0070006

metalloaminopeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000161491

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0004177

aminopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0031

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Ben-Bassat, A et al. (1987) Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169 751-7 PubMed GONUTS page
  2. Chai, SC et al. (2008) FE(II) is the native cofactor for Escherichia coli methionine aminopeptidase. J. Biol. Chem. 283 26879-85 PubMed GONUTS page
  3. Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  4. Watt, RM et al. (2007) Visualizing the proteome of Escherichia coli: an efficient and versatile method for labeling chromosomal coding DNA sequences (CDSs) with fluorescent protein genes. Nucleic Acids Res. 35 e37 PubMed GONUTS page
  5. Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page