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Protein

Long-chain-fatty-acid--CoA ligase

Gene

fadD

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids.By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi213 – 22412ATPCuratedAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL386585:GJFA-2487-MONOMER.
ECOO157:FADD-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase
Short name:
Acyl-CoA synthetase
Gene namesi
Name:fadD
Synonyms:oldD
Ordered Locus Names:Z2848, ECs2514
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558 Componenti: Chromosome UP000002519 Componenti: Chromosome

Subcellular locationi

  1. Membrane Curated; Peripheral membrane protein Curated

  2. Note: Partially membrane-associated.Curated

GO - Cellular componenti

  1. membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 561561Long-chain-fatty-acid--CoA ligasePRO_0000193127Add
BLAST

Interactioni

Subunit structurei

Homodimer.Curated

Protein-protein interaction databases

STRINGi155864.Z2848.

Structurei

3D structure databases

ProteinModelPortaliQ8XDR6.
SMRiQ8XDR6. Positions 23-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000229983.
KOiK01897.
OMAiCNPATID.
OrthoDBiEOG6MH5BV.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8XDR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT
60 70 80 90 100
FRKLEERSRA FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI
110 120 130 140 150
VVNVNPLYTP RELEHQLNDS GASAIVIVSN FAHTLEKVVD KTAVQHVILT
160 170 180 190 200
RMGDQLSTAK GTLVNFVVKY IKRLVPKYHL PDAISFRSAL HNGYRMQYVK
210 220 230 240 250
PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA TYGPLLHPGK
260 270 280 290 300
ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF
310 320 330 340 350
TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG
360 370 380 390 400
QYLLEGYGLT ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVS
410 420 430 440 450
PGQPGELCVR GPQVMLGYWQ RPDATDEIIK NGWLHTGDIA VMDEEGFLRI
460 470 480 490 500
VDRKKDMILV SGFNVYPNEI EDVVMQHPGV QEVAAVGVPS GSSGEAVKIF
510 520 530 540 550
VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN VGKILRRELR
560
DEARGKVDNK A
Length:561
Mass (Da):62,364
Last modified:March 1, 2002 - v1
Checksum:i4DE944AB7DF40CF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56794.1.
BA000007 Genomic DNA. Translation: BAB35937.1.
PIRiB90943.
F85791.
RefSeqiNP_288241.1. NC_002655.2.
NP_310541.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56794; AAG56794; Z2848.
BAB35937; BAB35937; BAB35937.
GeneIDi912449.
961778.
KEGGiece:Z2848.
ecs:ECs2514.
PATRICi18354390. VBIEscCol44059_2406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56794.1.
BA000007 Genomic DNA. Translation: BAB35937.1.
PIRiB90943.
F85791.
RefSeqiNP_288241.1. NC_002655.2.
NP_310541.1. NC_002695.1.

3D structure databases

ProteinModelPortaliQ8XDR6.
SMRiQ8XDR6. Positions 23-551.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z2848.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG56794; AAG56794; Z2848.
BAB35937; BAB35937; BAB35937.
GeneIDi912449.
961778.
KEGGiece:Z2848.
ecs:ECs2514.
PATRICi18354390. VBIEscCol44059_2406.

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000229983.
KOiK01897.
OMAiCNPATID.
OrthoDBiEOG6MH5BV.

Enzyme and pathway databases

BioCyciECOL386585:GJFA-2487-MONOMER.
ECOO157:FADD-MONOMER.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiLCFA_ECO57
AccessioniPrimary (citable) accession number: Q8XDR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Activity is the highest with fatty acid substrates of > 10 carbon atoms.By similarity

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.