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ECOLI:LDCI

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) cadA (synonyms: ldcI)
Protein Name(s) Lysine decarboxylase, inducible

LDC

External Links
UniProt P0A9H3
EMBL M76411
U14003
U00096
AP009048
M67452
PIR B41842
RefSeq NP_418555.1
YP_492275.1
PDB 3N75
3Q16
4UPB
4UPF
PDBsum 3N75
3Q16
4UPB
4UPF
ProteinModelPortal P0A9H3
SMR P0A9H3
DIP DIP-35646N
IntAct P0A9H3
MINT MINT-1234345
STRING 511145.b4131
PaxDb P0A9H3
EnsemblBacteria AAC77092
BAE78134
GeneID 12931783
948643
KEGG ecj:Y75_p4019
eco:b4131
PATRIC 32123829
EchoBASE EB0129
EcoGene EG10131
eggNOG COG1982
HOGENOM HOG000164394
InParanoid P0A9H3
KO K01582
OMA VKPRVMT
OrthoDB EOG696BRZ
PhylomeDB P0A9H3
BioCyc EcoCyc:LYSDECARBOX-MONOMER
ECOL316407:JW4092-MONOMER
MetaCyc:LYSDECARBOX-MONOMER
EvolutionaryTrace P0A9H3
PRO PR:P0A9H3
Proteomes UP000000318
UP000000625
Genevestigator P0A9H3
GO GO:0005737
GO:0042802
GO:0008923
GO:0030170
GO:0006554
Gene3D 3.40.640.10
3.90.100.10
3.90.1150.10
InterPro IPR005308
IPR011193
IPR000310
IPR008286
IPR015424
IPR015421
IPR015422
Pfam PF01276
PF03711
PF03709
PIRSF PIRSF009393
SUPFAM SSF53383
SSF55904
PROSITE PS00703

Annotations

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

enables

GO:0042802

identical protein binding

PMID:21278708[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9H3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:21148420[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9H3

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16301313[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A9H3

F

Seeded From UniProt

complete

enables

GO:0008923

lysine decarboxylase activity

PMID:9226257[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006554

lysine catabolic process

PMID:9226257[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0097216

guanosine tetraphosphate binding

PMID:21278708[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008923

lysine decarboxylase activity

PMID:6767710[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008923

lysine decarboxylase activity

PMID:16301313[3]

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:IPR000310
InterPro:IPR008286
InterPro:IPR015421
InterPro:IPR015422
InterPro:IPR036633

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011193

C

Seeded From UniProt

complete

involved_in

GO:0006520

cellular amino acid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011193

P

Seeded From UniProt

complete

enables

GO:0016831

carboxy-lyase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005308
InterPro:IPR011193

F

Seeded From UniProt

complete

enables

GO:0008923

lysine decarboxylase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.1.1.18

F

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

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

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

Notes

References

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

  1. 1.0 1.1 Kanjee, U et al. (2011) Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase. EMBO J. 30 931-44 PubMed GONUTS page
  2. El Bakkouri, M et al. (2010) Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. Proc. Natl. Acad. Sci. U.S.A. 107 22499-504 PubMed GONUTS page
  3. 3.0 3.1 Snider, J et al. (2006) Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase. J. Biol. Chem. 281 1532-46 PubMed GONUTS page
  4. 4.0 4.1 Kikuchi, Y et al. (1997) Characterization of a second lysine decarboxylase isolated from Escherichia coli. J. Bacteriol. 179 4486-92 PubMed GONUTS page
  5. Goldemberg, SH (1980) Lysine decarboxylase mutants of Escherichia coli: evidence for two enzyme forms. J. Bacteriol. 141 1428-31 PubMed GONUTS page