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Q93Q12

- FADB_PSEOL

UniProt

Q93Q12 - FADB_PSEOL

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Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB
Organism
Pseudomonas oleovorans
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Important for catalytic activity By similarity
Sitei140 – 1401Important for catalytic activity By similarity
Binding sitei297 – 2971Substrate By similarity
Binding sitei325 – 3251NAD; via amide nitrogen By similarity
Binding sitei344 – 3441NAD By similarity
Binding sitei408 – 4081NAD By similarity
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activity By similarity
Binding sitei454 – 4541NAD By similarity
Binding sitei501 – 5011Substrate By similarity
Binding sitei660 – 6601Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NAD By similarity
Nucleotide bindingi428 – 4303NAD By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
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)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadB
OrganismiPseudomonas oleovorans
Taxonomic identifieri301 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas oleovorans/pseudoalcaligenes group

Subcellular locationi

GO - Cellular componenti

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Fatty acid oxidation complex subunit alphaUniRule annotation
PRO_0000109277Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA) By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ93Q12.
SMRiQ93Q12. Positions 1-714.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomerase By similarity
Add
BLAST
Regioni312 – 7154043-hydroxyacyl-CoA dehydrogenase By similarity
Add
BLAST

Sequence similaritiesi

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.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 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]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93Q12-1 [UniParc]FASTAAdd to Basket

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MIYQGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIQAD    50
ASVKGVIVSS GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE 100
DLEVPTVAAI SGIALGGGLE MCLAADYRVM STSAKIGLPE VKLGIYPGFG 150
GTVRLPRLIG SDNAIEWIAA GKENRAEDAL KVGAVDAVVA PELLMAGALD 200
LVKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP 250
APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSVAESL IGLFLNDQEL 300
KRKAKAHDEI AHDAKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI 350
QLGLNEASKL LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA 400
VVENPKVKQA VLAEVETQVK DDAILASNTS TISINLLAKA LKRPENFVGM 450
HFFNPVHMMP LVEVIRGEKS SEVAVATTVA YAKKMGKNPI VVNDCPGFLV 500
NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH 550
HGRDVMAEGF PDRMKDERRS AVDALYEANR LGQKNGKGFY AYETDKRGKP 600
KKVADASVLD VLKPIVFEQR EVTDEDIINW MMIPLCLETV RCLEDGIVET 650
AAEADMGLVY GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT 700
AKLREMAKNG QRFFN 715
Length:715
Mass (Da):77,268
Last modified:December 1, 2001 - v1
Checksum:iF67EE0D424E39307
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF288535 Genomic DNA. Translation: AAK83058.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF288535 Genomic DNA. Translation: AAK83058.1 .

3D structure databases

ProteinModelPortali Q93Q12.
SMRi Q93Q12. Positions 1-714.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00659 .

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 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 ]
Pfami PF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiFADB_PSEOL
AccessioniPrimary (citable) accession number: Q93Q12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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