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Q9HZJ2

- FADB_PSEAE

UniProt

Q9HZJ2 - FADB_PSEAE

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Protein
Fatty acid oxidation complex subunit alpha
Gene
fadB, PA3014
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
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

BioCyciMetaCyc:MONOMER-17591.
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
Ordered Locus Names:PA3014
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA3014.

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_0000109274Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi208964.PA3014.

Structurei

3D structure databases

ProteinModelPortaliQ9HZJ2.
SMRiQ9HZJ2. Positions 1-715.

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.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiNPIVVND.
OrthoDBiEOG6M9F0M.
PhylomeDBiQ9HZJ2.

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.

Q9HZJ2-1 [UniParc]FASTAAdd to Basket

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MIYQGKAITV KPLEGGIVEL NFDLKGESVN KFNRLTLSEL RAAVDAIKAD    50
ASVKGVIVTS GKDVFIVGAD ITEFVDNFQL PDEELMAGNL EANKIFSDFE 100
DLDVPTVAAI NGIALGGGLE MCLAADFRVM SATAKVGLPE VKLGIYPGFG 150
GTVRLPRLIG CDNAVEWIAS GKENKAEDAL KVGAVDAVVA PEQLQAAALD 200
LAKRAVAGEL DHKARRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP 250
APVEAIKSIQ KAANFGRDKA LEVEAAGFVK LAKTSVAQSL IGLFLNDQEL 300
KKKAKKYDEV AKDVKLAAVL GAGIMGGGIA YQSALKGTPI LMKDIREEGI 350
QMGLNEAAKL LGKRVEKGRL TPAKMAEALN GIRPTMSYGD FGNVDIVVEA 400
VVENPKVKQA VLAEVEGAVK EDAIIASNTS TISISLLAQA LKRPENFCGM 450
HFFNPVHMMP LVEVIRGEKT GETAIATTVA YAKKMGKSPI VVNDCPGFLV 500
NRVLFPYFGG FAKLLSFGVD FVRIDKVMEK FGWPMGPAYL SDVVGIDTGH 550
HGRDVMAEGF PDRMAVEGKT AVDVMYEANR LGQKNGKGFY AYETDKRGKP 600
KKVTDPQAYE VLKPIVVEQR EVTDEDIVNF MMIPLCLETV RCLEDGIVET 650
AAEADMGLIY GIGFPPFRGG ALRYIDSIGV AEFVALADKY AELGALYHPT 700
AKLREMAKNG QKFFG 715
Length:715
Mass (Da):76,954
Last modified:March 1, 2001 - v1
Checksum:i7ED8573BE8F31101
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG06402.1.
PIRiG83269.
RefSeqiNP_251704.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG06402; AAG06402; PA3014.
GeneIDi878680.
KEGGipae:PA3014.
PATRICi19840585. VBIPseAer58763_3162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG06402.1 .
PIRi G83269.
RefSeqi NP_251704.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q9HZJ2.
SMRi Q9HZJ2. Positions 1-715.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA3014.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG06402 ; AAG06402 ; PA3014 .
GeneIDi 878680.
KEGGi pae:PA3014.
PATRICi 19840585. VBIPseAer58763_3162.

Organism-specific databases

PseudoCAPi PA3014.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi NPIVVND.
OrthoDBi EOG6M9F0M.
PhylomeDBi Q9HZJ2.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:MONOMER-17591.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiFADB_PSEAE
AccessioniPrimary (citable) accession number: Q9HZJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 94 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, Reference proteome

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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