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A1JIG4 (FADB_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. 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:YE0268
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length729 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 – 729729Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_1000069584

Regions

Nucleotide binding400 – 4023NAD By similarity
Nucleotide binding427 – 4293NAD By similarity
Region1 – 189189Enoyl-CoA hydratase/isomerase By similarity
Region311 – 7294193-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
A1JIG4 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: E60AAF8162634C1A

FASTA72978,871
        10         20         30         40         50         60 
MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTQTVANLG EALVVLEKQS ELKGLLLRSA 

        70         80         90        100        110        120 
KAAFIVGADI TEFLSLFNEP PEKLHQWLVF ANDIFNRLED LPVPTIAAIN GYALGGGCEC 

       130        140        150        160        170        180 
ILATDFRVAS PEARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIAAG KDIIAKDALK 

       190        200        210        220        230        240 
VGLVDAVVAP EKLVDAALSI LNQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGMV 

       250        260        270        280        290        300 
MQVAGKHYPA PLTAVKTIEA AAKFGRAEAL ILETNSFVPL AGSNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
GQAKKLSKGV SAPKQAAVLG AGIMGGGIAY QSALKGVPVI MKDINDKSLT LGMNEAAKLL 

       370        380        390        400        410        420 
NKQLERGKID GLKMANILAT IQPTLDYAGI ERAQVIVEAV VENPKVKAAV LAEVETLIGE 

       430        440        450        460        470        480 
ETVLASNTST IPIDQLAKSL KRPENFCGMH FFNPVHRMPL VEIIRGTKTS DKTIAAVVAY 

       490        500        510        520        530        540 
ATQMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLVRDGADF RQIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAVGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDTKGKP 

       610        620        630        640        650        660 
RKENDEQVDA LLAQVSQPLQ KFSDDDIIAR TMIPMINEVV RCLEEGIIAS PAEGDMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG VFRYLDTIGS ANYVEMAQRY THLGALYQVP PGLRAKAEHN ESYYPVAAAL 


LDVSISQPA 

« Hide

References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL10402.1.
RefSeqYP_001004653.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JIG4.
SMRA1JIG4. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE0268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL10402; CAL10402; YE0268.
GeneID4714532.
KEGGyen:YE0268.
PATRIC18559901. VBIYerEnt11519_0360.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261344.
KOK01825.
OMAAKGMVMQ.
OrthoDBEOG6M9F0M.

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.
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.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02437. FadB. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADB_YERE8
AccessionPrimary (citable) accession number: A1JIG4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 60 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