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

Q66FR8 (FADB_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:YPTB0267
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [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_0000109296

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
Q66FR8 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 2CC3F4F962ED3791

FASTA72978,798
        10         20         30         40         50         60 
MLYQSETLQL HWLENGIAEL VFDAPGSVNK LDTKTVANLG EALNVLEKQS ELKGLLLRSA 

        70         80         90        100        110        120 
KTALIVGADI TEFLSLFNAP PEKLHQWLVF ANTIFNRLED LPVPTISAIN GYALGGGCEC 

       130        140        150        160        170        180 
ILATDFRIAS PEARIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIATG KDVTANDALK 

       190        200        210        220        230        240 
IGLVDAVVDP EKLVGSALTM LKQAIDGKLD WQAARRPKLE PLKLNPTEAA MCFTIAKGRV 

       250        260        270        280        290        300 
MQVAGKHYPA PLTAVKTIEA AAKFGRTEAL NLETNSFVPL AGSNEARALV GIFLNDQYVK 

       310        320        330        340        350        360 
AQAKKLSKGV AAPKLAAVLG AGIMGGGIAY QSALKSVPVI MKDINENSLD LGMNEAAKLL 

       370        380        390        400        410        420 
NKQLERGKVD GLKMASILAT IRPTLDYAGI ERAQVIVEAV VENPKVKAAV LAEVEALIGE 

       430        440        450        460        470        480 
DTVLASNTST IPIDQLAKSL KRPENFCGMH FFNPVHQMPL VEIIRGAKTS DKTLAAVVAY 

       490        500        510        520        530        540 
ATQMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLVRDGGDF HQIDKVMEKQ FGWPMGPAYL 

       550        560        570        580        590        600 
LDVVGIDTAH HAQAVMAAGF PERMNKDYRD AVDVMFDNQR FGQKNGQGFY RYTQDAKGKP 

       610        620        630        640        650        660 
RKENDEQVDK LLAEISQPLQ EFSDEDIIAR TMIPMINEVV RCLEEGIIAS AAEGDMALVY 

       670        680        690        700        710        720 
GLGFPPFHGG VFRYLDTLGS ANYVEMAQRY AHLGALYHVP AGLRAKAEHN ESYYPVAAAL 


LDVSTNQPA 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH19507.1.
RefSeqYP_068813.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66FR8.
SMRQ66FR8. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB0267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH19507; CAH19507; YPTB0267.
GeneID2955522.
KEGGyps:YPTB0267.
PATRIC18638639. VBIYerPse22266_0432.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycYPSE273123:GI1M-284-MONOMER.
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. 1 hit.
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_YERPS
AccessionPrimary (citable) accession number: Q66FR8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 72 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