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ECOLI:PLDB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pldB
Protein Name(s) Lysophospholipase L2

Lecithinase B

External Links
UniProt P07000
EMBL X03155
M87049
U00096
AP009048
PIR B65187
RefSeq YP_026266.1
YP_491617.1
ProteinModelPortal P07000
SMR P07000
IntAct P07000
STRING 511145.b3825
PaxDb P07000
PRIDE P07000
EnsemblBacteria AAT48224
BAE77476
GeneID 12933622
948314
KEGG ecj:Y75_p3353
eco:b3825
PATRIC 32123151
EchoBASE EB0732
EcoGene EG10739
eggNOG COG2267
HOGENOM HOG000285163
InParanoid P07000
KO K01048
OMA YHWVREG
OrthoDB EOG6CCH34
PhylomeDB P07000
BioCyc EcoCyc:EG10739-MONOMER
ECOL316407:JW5584-MONOMER
PRO PR:P07000
Proteomes UP000000318
UP000000625
Genevestigator P07000
GO GO:0016020
GO:0005886
GO:0004622
GO:0006629
Gene3D 3.40.50.1820
InterPro IPR029058
IPR000073
Pfam PF00561
SUPFAM SSF53474

Annotations

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

part_of

GO:0016020

membrane

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10739
PANTHER:PTN000177089
SGD:S000001577

C

Seeded From UniProt

complete

enables

GO:0004622

lysophospholipase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10739
PANTHER:PTN001699633

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:3908447[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004622

lysophospholipase activity

PMID:3908447[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016747

transferase activity, transferring acyl groups other than amino-acyl groups

PMID:1649829[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016747

transferase activity, transferring acyl groups other than amino-acyl groups

PMID:3908447[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004622

lysophospholipase activity

PMID:3908447[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004622

lysophospholipase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.5

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

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

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. 2.0 2.1 2.2 2.3 Karasawa, K et al. (1985) Purification and characterization of lysophospholipase L2 of Escherichia coli K-12. J. Biochem. 98 1117-25 PubMed GONUTS page
  3. Hsu, L et al. (1991) Isolation and characterization of Escherichia coli K-12 mutants lacking both 2-acyl-glycerophosphoethanolamine acyltransferase and acyl-acyl carrier protein synthetase activity. J. Biol. Chem. 266 13783-8 PubMed GONUTS page