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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas aeruginosa (strain PA7)
Status
Reviewed-Annotation score: 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.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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei120Important for catalytic activityUniRule annotation1
Sitei140Important for catalytic activityUniRule annotation1
Binding sitei297SubstrateUniRule annotation1
Binding sitei325NAD; via amide nitrogenUniRule annotation1
Binding sitei344NADUniRule annotation1
Binding sitei408NADUniRule annotation1
Binding sitei430NADUniRule annotation1
Active sitei451For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation1
Binding sitei454NADUniRule annotation1
Binding sitei501SubstrateUniRule annotation1
Binding sitei660SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi401 – 403NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

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 alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadBUniRule annotation
Ordered Locus Names:PSPA7_2145
OrganismiPseudomonas aeruginosa (strain PA7)
Taxonomic identifieri381754 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000001582 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000695651 – 715Fatty acid oxidation complex subunit alphaAdd BLAST715

Proteomic databases

PRIDEiA6V382.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA6V382.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST190
Regioni312 – 7153-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST404

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261344.
KOiK01825.
OMAiYKAKRQP.

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. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
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. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A6V382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQGKAITV KPLEGGIVEL NFDLKGESVN KFNRLTLSEL RAAVDAIKAD
60 70 80 90 100
AAVKGVIVTS GKDVFIVGAD ITEFVDNFQL PDEELMAGNL EANKIFSDFE
110 120 130 140 150
DLDVPTVAAI NGIALGGGLE MCLAADFRVM SATAKVGLPE VKLGIYPGFG
160 170 180 190 200
GTVRLPRLIG CDNAVEWIAS GKENKAEDAL KVGAVDAVVA PEQLQAAALD
210 220 230 240 250
LAKRAVAGEL DHKARRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP
260 270 280 290 300
APVEAIKSIQ KAANFGRDKA LEVEAAGFVK LAKTSVAQSL IGLFLNDQEL
310 320 330 340 350
KKKAKKYDEV AKDVKLAAVL GAGIMGGGIA YQSALKGTPI LMKDIREEGI
360 370 380 390 400
QMGLNEAAKL LGKRVEKGRL TPAKMAEALN GIRPTMSYGD FGNVDIVVEA
410 420 430 440 450
VVENPKVKQA VLAEVEGAVK EDAIIASNTS TISISLLAQA LKRPENFCGM
460 470 480 490 500
HFFNPVHMMP LVEVIRGEKT GETAIATTVA YAKKMGKSPI VVNDCPGFLV
510 520 530 540 550
NRVLFPYFGG FAKLLGFGVD FVRIDKVMEK FGWPMGPAYL SDVVGIDTGH
560 570 580 590 600
HGRDVMAEGF PDRMAVEGKT AVDVMYEANR LGQKNGKGFY AYETDKRGKP
610 620 630 640 650
KKVTDPQAYE VLKPIVVEQR EVTDEDIVNF MMIPLCLETV RCLEDGIVET
660 670 680 690 700
AAEADMGLIY GIGFPPFRGG ALRYIDSIGV AEFVALADKY AELGALYHPT
710
AKLREMAKNG QKFFG
Length:715
Mass (Da):76,908
Last modified:August 21, 2007 - v1
Checksum:i8EB3FA1EAA8234E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000744 Genomic DNA. Translation: ABR83067.1.
RefSeqiWP_012075144.1. NC_009656.1.

Genome annotation databases

EnsemblBacteriaiABR83067; ABR83067; PSPA7_2145.
KEGGipap:PSPA7_2145.
PATRICi19826072. VBIPseAer80442_2060.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000744 Genomic DNA. Translation: ABR83067.1.
RefSeqiWP_012075144.1. NC_009656.1.

3D structure databases

ProteinModelPortaliA6V382.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA6V382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR83067; ABR83067; PSPA7_2145.
KEGGipap:PSPA7_2145.
PATRICi19826072. VBIPseAer80442_2060.

Phylogenomic databases

HOGENOMiHOG000261344.
KOiK01825.
OMAiYKAKRQP.

Enzyme and pathway databases

UniPathwayiUPA00659.

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. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
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. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADB_PSEA7
AccessioniPrimary (citable) accession number: A6V382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: November 2, 2016
This is version 72 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

Complete proteome, Multifunctional enzyme

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.