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ECOLI:DCDA

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) lysA
Protein Name(s) Diaminopimelate decarboxylase

DAP decarboxylase DAPDC

External Links
UniProt P00861
EMBL J01614
U29581
U00096
AP009048
PIR A01078
RefSeq NP_417315.1
YP_491043.1
PDB 1KNW
1KO0
PDBsum 1KNW
1KO0
ProteinModelPortal P00861
SMR P00861
DIP DIP-10132N
IntAct P00861
MINT MINT-1292495
STRING 511145.b2838
SWISS-2DPAGE P00861
PaxDb P00861
PRIDE P00861
EnsemblBacteria AAC75877
BAE76907
GeneID 12932897
947313
KEGG ecj:Y75_p2772
eco:b2838
PATRIC 32121094
EchoBASE EB0544
EcoGene EG10549
eggNOG COG0019
HOGENOM HOG000045070
InParanoid P00861
KO K01586
OMA VVGYICE
OrthoDB EOG6Z9B18
PhylomeDB P00861
BioCyc EcoCyc:DIAMINOPIMDECARB-MONOMER
ECOL316407:JW2806-MONOMER
MetaCyc:DIAMINOPIMDECARB-MONOMER
UniPathway UPA00034
EvolutionaryTrace P00861
PRO PR:P00861
Proteomes UP000000318
UP000000625
Genevestigator P00861
GO GO:0008836
GO:0030170
GO:0009089
Gene3D 2.40.37.10
3.20.20.10
HAMAP MF_02120
InterPro IPR009006
IPR002986
IPR022643
IPR022657
IPR022644
IPR022653
IPR000183
IPR029066
Pfam PF02784
PF00278
PRINTS PR01181
PR01179
SUPFAM SSF50621
SSF51419
TIGRFAMs TIGR01048
PROSITE PS00878
PS00879

Annotations

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

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10549
PANTHER:PTN000159906
UniProtKB:P9WIU7

P

Seeded From UniProt

complete

enables

GO:0008836

diaminopimelate decarboxylase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10549
PANTHER:PTN000159906
TAIR:locus:2091055
TAIR:locus:2143054
UniProtKB:P19572
UniProtKB:P9WIU7

F

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

PMID:11856852[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

PMID:4926684[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008836

diaminopimelate decarboxylase activity

PMID:14343156[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008836

diaminopimelate decarboxylase activity

PMID:10625645[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000183
InterPro:IPR009006
InterPro:IPR022643
InterPro:IPR022644

F

Seeded From UniProt

complete

enables

GO:0008836

diaminopimelate decarboxylase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002986

F

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002986

P

Seeded From UniProt

complete

enables

GO:0008836

diaminopimelate decarboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.1.20

F

Seeded From UniProt

complete

enables

GO:0030170

pyridoxal phosphate binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000160031

F

Seeded From UniProt

complete

enables

GO:0008836

diaminopimelate decarboxylase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000160031

F

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000160031

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0210

F

Seeded From UniProt

complete

involved_in

GO:0009085

lysine biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0457

P

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00034

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. Momany, C et al. (2002) Crystallization of diaminopimelate decarboxylase from Escherichia coli, a stereospecific D-amino-acid decarboxylase. Acta Crystallogr. D Biol. Crystallogr. 58 549-52 PubMed GONUTS page
  3. Bukhari, AI & Taylor, AL (1971) Genetic analysis of diaminopimelic acid- and lysine-requiring mutants of Escherichia coli. J. Bacteriol. 105 844-54 PubMed GONUTS page
  4. WHITE, PJ & KELLY, B (1965) PURIFICATION AND PROPERTIES OF DIAMINOPIMELATE DECARBOXYLASE FROM ESCHERICHIA COLI. Biochem. J. 96 75-84 PubMed GONUTS page
  5. Bourot, S et al. (2000) Glycine betaine-assisted protein folding in a lysA mutant of Escherichia coli. J. Biol. Chem. 275 1050-6 PubMed GONUTS page