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Q93Q12 (FADB_PSEOL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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
OrganismPseudomonas oleovorans
Taxonomic identifier301 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas oleovorans/pseudoalcaligenes group

Protein attributes

Sequence length715 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 – 715715Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01621
PRO_0000109277

Regions

Nucleotide binding401 – 4033NAD By similarity
Nucleotide binding428 – 4303NAD By similarity
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 By similarity
Binding site3251NAD; via amide nitrogen By similarity
Binding site3441NAD By similarity
Binding site4081NAD By similarity
Binding site4541NAD By similarity
Binding site5011Substrate By similarity
Binding site6601Substrate By similarity
Site1201Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93Q12 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F67EE0D424E39307

FASTA71577,268
        10         20         30         40         50         60 
MIYQGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIQAD ASVKGVIVSS 

        70         80         90        100        110        120 
GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE DLEVPTVAAI SGIALGGGLE 

       130        140        150        160        170        180 
MCLAADYRVM STSAKIGLPE VKLGIYPGFG GTVRLPRLIG SDNAIEWIAA GKENRAEDAL 

       190        200        210        220        230        240 
KVGAVDAVVA PELLMAGALD LVKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF 

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

       310        320        330        340        350        360 
KRKAKAHDEI AHDAKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL 

       370        380        390        400        410        420 
LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA VVENPKVKQA VLAEVETQVK 

       430        440        450        460        470        480 
DDAILASNTS TISINLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SEVAVATTVA 

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

       550        560        570        580        590        600 
MDVVGIDTGH HGRDVMAEGF PDRMKDERRS AVDALYEANR LGQKNGKGFY AYETDKRGKP 

       610        620        630        640        650        660 
KKVADASVLD VLKPIVFEQR EVTDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLVY 

       670        680        690        700        710 
GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT AKLREMAKNG QRFFN 

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References

[1]"The role of the fatty acid beta-oxidation multienzyme complex from Pseudomonas oleovorans in polyhydroxyalkanoate biosynthesis: molecular characterization of the fadBA operon from P. oleovorans and of the enoyl-CoA hydratase genes phaJ from P. oleovorans and Pseudomonas putida."
Fiedler S., Steinbuchel A., Rehm B.H.
Arch. Microbiol. 178:149-160(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 29347 / NRRL B-14683 / TF4-1L.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF288535 Genomic DNA. Translation: AAK83058.1.

3D structure databases

ProteinModelPortalQ93Q12.
SMRQ93Q12. Positions 1-714.
ModBaseSearch...
MobiDBSearch...

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.
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_PSEOL
AccessionPrimary (citable) accession number: Q93Q12
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 74 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