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

P28793 (FADB_PSEFR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:faoA
OrganismPseudomonas fragi
Taxonomic identifier296 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length715 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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). Ref.3

Induction

By palmitic acid. Ref.2

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

fadAP287903EBI-1039318,EBI-1039311

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 715715Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109276

Regions

Nucleotide binding401 – 4033NAD HAMAP-Rule MF_01621
Nucleotide binding428 – 4303NAD HAMAP-Rule MF_01621
Region1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Region312 – 7154043-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Active site4511For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding site2971Substrate
Binding site3251NAD; via amide nitrogen
Binding site3441NAD
Binding site4081NAD
Binding site4541NAD
Binding site5011Substrate
Binding site6601Substrate
Site1201Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

Secondary structure

............................................................................................................................ 715
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28793 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: F22727CDEF7F3DB5

FASTA71577,137
        10         20         30         40         50         60 
MIYEGKAITV TALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIKAD ASVKGVIVSS 

        70         80         90        100        110        120 
GKDVFIVGAD ITEFVENFKL PDAELIAGNL EANKIFSDFE DLNVPTVAAI NGIALGGGLE 

       130        140        150        160        170        180 
MCLAADFRVM ADSAKIGLPE VKLGIYPGFG GTVRLPRLIG VDNAVEWIAS GKENRAEDAL 

       190        200        210        220        230        240 
KVSAVDAVVT ADKLGAAALD LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF 

       250        260        270        280        290        300 
VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSASNCL IGLFLNDQEL 

       310        320        330        340        350        360 
KKKAKVYDKI AKDVKQAAVL GAGIMGGGIA YQSASKGTPI LMKDINEHGI EQGLAEAAKL 

       370        380        390        400        410        420 
LVGRVDKGRM TPAKMAEVLN GIRPTLSYGD FGNVDLVVEA VVENPKVKQA VLAEVENHVR 

       430        440        450        460        470        480 
EDAILASNTS TISISLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SDLAVATTVA 

       490        500        510        520        530        540 
YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL 

       550        560        570        580        590        600 
MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS AIDALYEAKR LGQKNGKGFY AYEADKKGKQ 

       610        620        630        640        650        660 
KKLVDSSVLE VLKPIVYEQR DVTDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLVY 

       670        680        690        700        710 
GIGFPLFRGG ALRYIDSIGV AEFVALADQY AELGALYHPT AKLREMAKNG QSFFG 

« Hide

References

[1]"Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B-0771 which encode the two subunits of the HDT multienzyme complex involved in fatty acid beta-oxidation."
Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.
J. Biochem. 111:8-15(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: B-0771.
[2]"Transcription of the faoAB operon which encodes the HDT multienzyme complex involved in fatty acid beta-oxidation in Pseudomonas fragi B-0771."
Sato S., Ozeki Y., Kawaguchi A.
J. Biochem. 115:286-292(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[3]"Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex."
Ishikawa M., Tsuchiya D., Oyama T., Tsunaka Y., Morikawa K.
EMBO J. 23:2745-2754(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH NAD AND ACYL-COENZYME A, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10390 Genomic DNA. Translation: BAA01227.1.
PIRJX0199.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WDKX-ray2.50A/B1-715[»]
1WDLX-ray3.50A/B1-715[»]
1WDMX-ray3.80A/B1-715[»]
2D3TX-ray3.40A/B1-715[»]
ProteinModelPortalP28793.
SMRP28793. Positions 1-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29089N.
IntActP28793. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. 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.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP28793.

Entry information

Entry nameFADB_PSEFR
AccessionPrimary (citable) accession number: P28793
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 11, 2014
This is version 104 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways