A0A093FWZ7 · A0A093FWZ7_ECOLX

  • Protein
    Fatty acid oxidation complex subunit alpha
  • Gene
    fadB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.

Catalytic activity

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site119Important for catalytic activity
Site139Important for catalytic activity
Binding site296substrate
Binding site324NAD+ (UniProtKB | ChEBI)
Binding site343NAD+ (UniProtKB | ChEBI)
Binding site400-402NAD+ (UniProtKB | ChEBI)
Binding site407NAD+ (UniProtKB | ChEBI)
Binding site429NAD+ (UniProtKB | ChEBI)
Active site450For 3-hydroxyacyl-CoA dehydrogenase activity
Binding site453NAD+ (UniProtKB | ChEBI)
Binding site500substrate
Binding site660substrate

GO annotations

AspectTerm
Cellular Componentfatty acid beta-oxidation multienzyme complex
Molecular Function3-hydroxyacyl-CoA dehydrogenase activity
Molecular Function3-hydroxybutyryl-CoA epimerase activity
Molecular Functiondelta(3)-delta(2)-enoyl-CoA isomerase activity
Molecular Functionenoyl-CoA hydratase activity
Molecular FunctionNAD+ binding
Biological Processfatty acid beta-oxidation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fatty acid oxidation complex subunit alpha

Including 2 domains:

  • Recommended name
    Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
  • EC number
  • Recommended name
    3-hydroxyacyl-CoA dehydrogenase
  • EC number

Gene names

    • Name
      fadB
    • ORF names
      BGZ_04743
      , C1Q91_004266
      , C3F40_16440
      , CF22_003756
      , CG704_18685
      , CV83915_02221
      , D4M65_18965
      , E5H86_14945
      , EPS97_18195
      , GAJ12_16745
      , GQE86_18185
      , H0O72_20630
      , HEP30_018310
      , HHH44_003634
      , HV109_23330
      , I6H02_14785
      , J5U05_003797
      , KQO22_003551
      , NCTC10429_00317
      , NCTC11181_02165
      , OFN31_18455

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 1199
    • WW601
    • CV839-15
    • ST-87-5
    • W1_5_ERB1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A093FWZ7

Proteomes

Interaction

Subunit

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-189Enoyl-CoA hydratase/isomerase
Region311-7293-hydroxyacyl-CoA dehydrogenase
Domain316-4943-hydroxyacyl-CoA dehydrogenase NAD binding
Domain496-5923-hydroxyacyl-CoA dehydrogenase C-terminal
Domain627-6913-hydroxyacyl-CoA dehydrogenase C-terminal
Region708-729Disordered

Sequence similarities

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.
In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    729
  • Mass (Da)
    79,549
  • Last updated
    2014-11-26 v1
  • Checksum
    E4BBE9FEDBE1E5B4
MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDVVVEAVVENPKVKKAVLAETEQKVRPDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP024978
EMBL· GenBank· DDBJ
ATZ32543.1
EMBL· GenBank· DDBJ
Genomic DNA
CP026399
EMBL· GenBank· DDBJ
AUY03207.1
EMBL· GenBank· DDBJ
Genomic DNA
AASCJS010000033
EMBL· GenBank· DDBJ
EFA9847801.1
EMBL· GenBank· DDBJ
Genomic DNA
AASEPP010000022
EMBL· GenBank· DDBJ
EFC2247075.1
EMBL· GenBank· DDBJ
Genomic DNA
AASWKX010000021
EMBL· GenBank· DDBJ
EFH6166682.1
EMBL· GenBank· DDBJ
Genomic DNA
AATJQG010000021
EMBL· GenBank· DDBJ
EFM0517706.1
EMBL· GenBank· DDBJ
Genomic DNA
ABAVVR010000045
EMBL· GenBank· DDBJ
EHQ1861317.1
EMBL· GenBank· DDBJ
Genomic DNA
DABALL010000023
EMBL· GenBank· DDBJ
HAH1420204.1
EMBL· GenBank· DDBJ
Genomic DNA
DADRWU010000044
EMBL· GenBank· DDBJ
HBA4248592.1
EMBL· GenBank· DDBJ
Genomic DNA
JABWMK020000034
EMBL· GenBank· DDBJ
MBB2468037.1
EMBL· GenBank· DDBJ
Genomic DNA
JAOVKC010000023
EMBL· GenBank· DDBJ
MCV5623732.1
EMBL· GenBank· DDBJ
Genomic DNA
WSXK01000055
EMBL· GenBank· DDBJ
MWF96970.1
EMBL· GenBank· DDBJ
Genomic DNA
JACCPE010000038
EMBL· GenBank· DDBJ
NZD15935.1
EMBL· GenBank· DDBJ
Genomic DNA
NNAF01000050
EMBL· GenBank· DDBJ
OZO77403.1
EMBL· GenBank· DDBJ
Genomic DNA
CP056794
EMBL· GenBank· DDBJ
QLY99319.1
EMBL· GenBank· DDBJ
Genomic DNA
CP065611
EMBL· GenBank· DDBJ
QPR02988.1
EMBL· GenBank· DDBJ
Genomic DNA
SCIU01000042
EMBL· GenBank· DDBJ
RXB26365.1
EMBL· GenBank· DDBJ
Genomic DNA
UFYN01000002
EMBL· GenBank· DDBJ
STD40689.1
EMBL· GenBank· DDBJ
Genomic DNA
UGEX01000001
EMBL· GenBank· DDBJ
STL74356.1
EMBL· GenBank· DDBJ
Genomic DNA
QYMS01000049
EMBL· GenBank· DDBJ
TXW74180.1
EMBL· GenBank· DDBJ
Genomic DNA
CABWJN010000005
EMBL· GenBank· DDBJ
VWN18671.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp