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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei118 – 1181Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule 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

BioCyciVPAR223926:GHK4-2265-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadJUniRule annotation
Ordered Locus Names:VP2208
OrganismiVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Taxonomic identifieri223926 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000002493 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 703703Fatty acid oxidation complex subunit alphaPRO_0000109312Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).UniRule annotation

Protein-protein interaction databases

STRINGi223926.VP2208.

Structurei

3D structure databases

ProteinModelPortaliQ87MM3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydrataseUniRule annotationAdd
BLAST
Regioni308 – 7033963-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPiMF_01617. FadJ.
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.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02440. FadJ. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q87MM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQKAFSLN VDEQNIAWLA IDVPNEKMNT LQAAFADEMK EIFAQLKDSS
60 70 80 90 100
GIKGMIIHSL KPDNFVAGAD VRMLEACTTA NEAQALAKQG QELFQQLSDL
110 120 130 140 150
PYPVVAAIHG PCLGGGLELA LACDYRVCTD FDKTRLGLPE VQLGLLPGSG
160 170 180 190 200
GTQRLPRLIG LLPSLDLILT GKQLRAKKAK KLGVVDACVP DTILLDVAKQ
210 220 230 240 250
FIDKGKNKGK KKQSTKEKLM SGSGLGRKLV FEQAAKKTNQ KTRGNYPATV
260 270 280 290 300
AILEVIQHGL EKGFAQGQEL EAKRFGELVM SSESKALRSI FFATTEMKKE
310 320 330 340 350
HGTDAQPAAV KKVGVLGGGL MGAGISHVTV AKAKVPVRIK DVSNDGVLNA
360 370 380 390 400
LNYNYKLFEK QRKRRILSKA DLQAKMLQLS GGVDFTSYNH IDVVIEAVFE
410 420 430 440 450
DLDLKQQMVA DIEANAKSET IFATNTSSLP IHKIAEKAER PENIVGLHYF
460 470 480 490 500
SPVEKMPLVE VIPHETTSDE TISTVVALAK KQGKTPIVVK DKAGFYVNRI
510 520 530 540 550
LAPYMNEAAH ILLANEPIEK LDGALLDFGF PVGPITLLDE VGVDIGAKIM
560 570 580 590 600
PILVNELGER FKGPDVFDIL LNDGRKGRKS GKGFYTYKGK KKEVDKSIYK
610 620 630 640 650
LLKLTPESKL SDNDIALRCV LPMLNEAVRC LDDGIIRSPR DGDIGAIFGI
660 670 680 690 700
GFPPFLGGPF RYMDQFGLKE LVEKMNEFAS KYGDRYAPCD GLLTRAGEGR

TFY
Length:703
Mass (Da):76,856
Last modified:June 1, 2003 - v1
Checksum:iA2A62EDC4047BA3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000031 Genomic DNA. Translation: BAC60471.1.
RefSeqiNP_798587.1. NC_004603.1.
WP_005479507.1. NC_004603.1.

Genome annotation databases

EnsemblBacteriaiBAC60471; BAC60471; BAC60471.
GeneIDi1189721.
KEGGivpa:VP2208.
PATRICi20142564. VBIVibPar50997_2111.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000031 Genomic DNA. Translation: BAC60471.1.
RefSeqiNP_798587.1. NC_004603.1.
WP_005479507.1. NC_004603.1.

3D structure databases

ProteinModelPortaliQ87MM3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223926.VP2208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC60471; BAC60471; BAC60471.
GeneIDi1189721.
KEGGivpa:VP2208.
PATRICi20142564. VBIVibPar50997_2111.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciVPAR223926:GHK4-2265-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPiMF_01617. FadJ.
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.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02440. FadJ. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
    Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
    Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RIMD 2210633.

Entry informationi

Entry nameiFADJ_VIBPA
AccessioniPrimary (citable) accession number: Q87MM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: May 27, 2015
This is version 86 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

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.