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Q8EKR9 (FADB_SHEON) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadB
Ordered Locus Names:SO_0021
OrganismShewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]
Taxonomic identifier211586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 By similarity. HAMAP-Rule MF_01621

Catalytic activity

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP-Rule MF_01621

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP-Rule MF_01621

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP-Rule MF_01621

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. HAMAP-Rule MF_01621

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01621

Subunit structure

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

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 716716Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109288

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7164063-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4501For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2961Substrate By similarity
Binding site3241NAD; via amide nitrogen By similarity
Binding site3431NAD By similarity
Binding site4071NAD By similarity
Binding site4531NAD By similarity
Binding site5001Substrate By similarity
Binding site6601Substrate By similarity
Site1191Important for catalytic activity By similarity
Site1391Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EKR9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: CD0786FD13FBFC3E

FASTA71676,693
        10         20         30         40         50         60 
MIYQSPTIQV ELLEDNIAKL CFNAPGSVNK FDRETLASLD AALDSIKQQS NIQALVLTSG 

        70         80         90        100        110        120 
KDTFIVGADI TEFLGLFAQD DAVLLSWVEQ ANAVFNKLED LPFPTASAIK GFALGGGCET 

       130        140        150        160        170        180 
ILATDFRIAD TTAKIGLPET KLGIIPGFGG TVRLPRVIGA DNALEWITTG NEQRAEDALK 

       190        200        210        220        230        240 
VGAVDAVVAP EALEVAAIQM LKDAVAEKLD WQARRQRKLS PLTLPKLEAM MSFTTAKGMV 

       250        260        270        280        290        300 
FSVAGKHYPA PMAAVNVVEQ AATKGRSDAL QIEHQAFIKL AKTDVAKALI GIFLNDQFVK 

       310        320        330        340        350        360 
GKAKKAGKLA KAVNSAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD LGLNEAAKLL 

       370        380        390        400        410        420 
SAQVARGRST PEKMAKVLNN ITPALEYAPV KHADVVVEAV VEHPKVKAQV LAEVEQYVSE 

       430        440        450        460        470        480 
DAIIASNTST ISISLLAKSM KKPERFCGMH FFNPVHKMPL VEVIRGEHSS EETIASVVAY 

       490        500        510        520        530        540 
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF NGLLAEGGDF AAIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGLDTGH HAQAVMAEGF PDRMGKSGND AIDVMFENKR LGQKNGKGFY AYSVDSRGKP 

       610        620        630        640        650        660 
KKDVDPTSYE LLKAAFGEQK AFDADEIIAR TMIPMIIETV RCLEEGIVAS PAEADMGLVY 

       670        680        690        700        710 
GLGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRALAANN GSYYQA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014299 Genomic DNA. Translation: AAN53108.1.
RefSeqNP_715663.1. NC_004347.2.

3D structure databases

ProteinModelPortalQ8EKR9.
SMRQ8EKR9. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211586.SO_0021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN53108; AAN53108; SO_0021.
GeneID1167919.
KEGGson:SO_0021.
PATRIC23519733. VBISheOne101494_0021.

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMANPIVVND.
OrthoDBEOG6M9F0M.
PhylomeDBQ8EKR9.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPMF_01621. FadB.
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_SHEON
AccessionPrimary (citable) accession number: Q8EKR9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways