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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
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

Pathway:ifatty 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei120 – 1201Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Binding sitei325 – 3251NAD; via amide nitrogenUniRule annotation
Binding sitei344 – 3441NADUniRule annotation
Binding sitei408 – 4081NADUniRule annotation
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei454 – 4541NADUniRule annotation
Binding sitei501 – 5011SubstrateUniRule annotation
Binding sitei660 – 6601SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NADUniRule annotation
Nucleotide bindingi428 – 4303NADUniRule annotation

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

BioCyciPAER208963:GI5K-2032-MONOMER.
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:PA14_25080
OrganismiPseudomonas aeruginosa (strain UCBPP-PA14)
Taxonomic identifieri208963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000653 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Fatty acid oxidation complex subunit alphaPRO_1000069566Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ02PH8.
SMRiQ02PH8. Positions 1-715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni312 – 7154043-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

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

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiIIDIWAR.
OrthoDBiEOG6M9F0M.

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.
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 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.

Q02PH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQGKAITV KPLEGGIVEL NFDLKGESVN KFNRLTLSEL RAAVDAIKAD
60 70 80 90 100
ASVKGVIVTS 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 FAKLLSFGVD 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):76,954
Last modified:November 14, 2006 - v1
Checksum:i7ED8573BE8F31101
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000438 Genomic DNA. Translation: ABJ12251.1.
RefSeqiWP_003091204.1. NC_008463.1.

Genome annotation databases

EnsemblBacteriaiABJ12251; ABJ12251; PA14_25080.
KEGGipau:PA14_25080.
PATRICi19850154. VBIPseAer79785_2036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000438 Genomic DNA. Translation: ABJ12251.1.
RefSeqiWP_003091204.1. NC_008463.1.

3D structure databases

ProteinModelPortaliQ02PH8.
SMRiQ02PH8. Positions 1-715.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ12251; ABJ12251; PA14_25080.
KEGGipau:PA14_25080.
PATRICi19850154. VBIPseAer79785_2036.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiIIDIWAR.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciPAER208963:GI5K-2032-MONOMER.

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.
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 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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UCBPP-PA14.

Entry informationi

Entry nameiFADB_PSEAB
AccessioniPrimary (citable) accession number: Q02PH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: July 22, 2015
This is version 67 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

External Data

Dasty 3

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 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.