Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B6EGU2 (FADB_ALISL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. 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:VSAL_I2974
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length726 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 – 726726Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_1000186031

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7264163-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
B6EGU2 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: E40B3EB8D2AFE361

FASTA72678,731
        10         20         30         40         50         60 
MIYQGENLSV DYIENGIAHL VFNAAGSVNK LNIATLRSLG EAIDVLYKQK DLQALLLSSG 

        70         80         90        100        110        120 
KSAFIVGADI TEFLGLFDTP EEELSDWLHQ ANVIFSRLED LPVPTLSAIT GFALGGGCEC 

       130        140        150        160        170        180 
VLATDFRLAD DTASIGLPET QLGIMPGWGG SVRLPRLIGA DPAMEVITTG KPKRAKDALK 

       190        200        210        220        230        240 
IGMVDGIVSR ETLIDASVSM LKQAIDGQLN WQQRREQKKA PIQLSPLEAA MSFNVAKGMI 

       250        260        270        280        290        300 
MKMAGKHYPA PLTAVKSIEQ SANMHRDDAL AIENKHFVAL TRTDVAKSLV GIFLNDQLVK 

       310        320        330        340        350        360 
SKAKQAVKNS EPVKNAAVLG AGIMGGGIAY QSASKGVPVL MKDIAQASLD LGMNEASKLL 

       370        380        390        400        410        420 
NKQLERGRLS GLKMAQVLSS ITPSLNYGGI ETKDVIVEAV VENPTIKAAV LAEVENEVNE 

       430        440        450        460        470        480 
HAILASNTST IPISLLAKSL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS QQTIDRVVAY 

       490        500        510        520        530        540 
ASQMGKTPIV VNDCPGFFVN RVLFPYFAGF SLLLRDGGNY QQIDKVMEKE FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAQGF PERMAKNGRD VIDAMFEDDR YGQKNGIGFY AYALDKKGKP 

       610        620        630        640        650        660 
KKNIDEKTNA IIATITDSTQ PYTSEQISAR MMIPMINEVI RCLDEGIIAS PAEADMALVY 

       670        680        690        700        710        720 
GLGFPPFKGG VFRYLDSIGL DTYLDMAKEF EQLSPVYQVP DSIKQKAAAG ECYYPAPKSS 


VSSPSV 

« Hide

References

[1]"The genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238 shows extensive evidence of gene decay."
Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.
BMC Genomics 9:616-616(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LFI1238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM178379 Genomic DNA. Translation: CAQ80658.1.
RefSeqYP_002264299.1. NC_011312.1.

3D structure databases

ProteinModelPortalB6EGU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316275.VSAL_I2974.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ80658; CAQ80658; VSAL_I2974.
GeneID6988472.
KEGGvsa:VSAL_I2974.
PATRIC20856496. VBIAliSal95923_3219.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMAAKGMVMQ.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11730.

Enzyme and pathway databases

UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 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.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR012799. FadB.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_ALISL
AccessionPrimary (citable) accession number: B6EGU2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 46 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