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SALTY:LCFA

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Species (Taxon ID) Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). (99287)
Gene Name(s) fadD
Protein Name(s) Long-chain-fatty-acid--CoA ligase

Long-chain acyl-CoA synthetase

External Links
UniProt P63521
EMBL AE006468
RefSeq NP_460774.1
WP_000758418.1
ProteinModelPortal P63521
STRING 99287.STM1818
PaxDb P63521
PRIDE P63521
EnsemblBacteria AAL20733
GeneID 1253337
KEGG stm:STM1818
PATRIC 32382159
eggNOG ENOG4105CEY
COG0318
HOGENOM HOG000229983
KO K01897
OMA ITFSDFH
PhylomeDB P63521
Proteomes UP000001014
GO GO:0016020
GO:0005524
GO:0102391
GO:0004467
InterPro IPR025110
IPR020845
IPR000873
Pfam PF00501
PF13193
PROSITE PS00455

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004467

long-chain fatty acid-CoA ligase activity

PMID:27974467[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Organism: Salmonella enterica (Salmonella typhimurium). Paper's Protein Name: Long-chain acyl-CoA synthetase (FadD). UniProt's Protein Name: Long-chain-fatty-acid--CoA ligase. The control of Figure 6 shows that long-chain acyl-CoA synthetase is involved with the activity of Acyl-CoA ligase.

complete
CACAO 12279

involved_in

GO:0001676

long-chain fatty acid metabolic process

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004467

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000873

F

Seeded From UniProt

complete

enables

GO:0004467

long-chain fatty acid-CoA ligase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.2.1.3

F

Seeded From UniProt

complete

enables

GO:0102391

decanoate-CoA ligase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:6.2.1.3

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

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:0016874

ligase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472
UniProtKB-SubCell:SL-0162

C

Seeded From UniProt

complete

involved_in

GO:0006631

fatty acid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0276

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

Notes

References

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

  1. Han, X et al. (2017) Cyclic AMP Inhibits the Activity and Promotes the Acetylation of Acetyl-CoA Synthetase through Competitive Binding to the ATP/AMP Pocket. J. Biol. Chem. 292 1374-1384 PubMed GONUTS page