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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Vibrio vulnificus (strain YJ016)
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: 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
Sitei118Important for catalytic activityUniRule annotation1
Sitei140Important for catalytic activityUniRule annotation1

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/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:VV2440
OrganismiVibrio vulnificus (strain YJ016)
Taxonomic identifieri196600 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000002675 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001093141 – 705Fatty acid oxidation complex subunit alphaAdd BLAST705

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ7MIS5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 190Enoyl-CoA hydrataseUniRule annotationAdd BLAST190
Regioni308 – 7053-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST398

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

HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiPOG091H00UW.

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. 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.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02440. FadJ. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7MIS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQKAFNLK IDEQNIAWLG IDVPNEKMNT LQAAFADEMK AIFAQLKDSS
60 70 80 90 100
GLKGLIVHSL KPDNFVAGAD VRMLEACKTA PEAEALARQG QELFQQLSDL
110 120 130 140 150
PYPVVAAIHG PCLGGGLELA LACDFRVCSD DDATRLGLPE VQLGLLPGSG
160 170 180 190 200
GTQRLPRLIG LLPSLDLILT GKQLRAKKAK KLGVVDACVP QTILLDVAKQ
210 220 230 240 250
FVEKGKKRAK QKVTTKEKLL SGSGLGRKFV FEQAAKKTHE KTRGNYPATV
260 270 280 290 300
AILQVIQHGL EKGMKQGLEL EAKRFGELVM SNESKALRSI FFATTEMKKE
310 320 330 340 350
TGSEAKPSKV GMVGVLGGGL MGAGISHVSV AKAKVPVRIK DVSNDGVLNA
360 370 380 390 400
LKYNYKLFDK QRKRRILSKA QLQSKMLQLS GGTDFTSFNR TDVVIEAVFE
410 420 430 440 450
DLSLKQQMVA DIEANAKPET IFATNTSSLP IHKIAEKAQR PENIVGLHYF
460 470 480 490 500
SPVEKMPLVE VIPHESTSEE TIATVVALAK KQGKTPIVVK DQAGFYVNRI
510 520 530 540 550
LAPYMNESAH ILLANEPIDK IDTALLDFGF PVGPITLLDE VGVDIGAKIM
560 570 580 590 600
PILVAELGAR FKGPDVFDVL LNDGRKGRKS GKGFYTYKGK KKEVDKSVYK
610 620 630 640 650
LLKLTPESKL SDNDIALRCV LPMLNEAVRC LDDGIIRSPR DGDIGAIFGI
660 670 680 690 700
GFPPFLGGPF RYMDQFGLKE LVEKMNQFAE KYGDRFAPCD GLLTRAGEGR

RFYDN
Length:705
Mass (Da):77,042
Last modified:December 15, 2003 - v1
Checksum:i268F855F5EB5DD68
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000037 Genomic DNA. Translation: BAC95204.1.
RefSeqiWP_011150894.1. NC_005139.1.

Genome annotation databases

EnsemblBacteriaiBAC95204; BAC95204; BAC95204.
GeneIDi2625248.
KEGGivvy:VV2440.
PATRICi20171726. VBIVibVul40472_2446.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000037 Genomic DNA. Translation: BAC95204.1.
RefSeqiWP_011150894.1. NC_005139.1.

3D structure databases

ProteinModelPortaliQ7MIS5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC95204; BAC95204; BAC95204.
GeneIDi2625248.
KEGGivvy:VV2440.
PATRICi20171726. VBIVibVul40472_2446.

Phylogenomic databases

HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiPOG091H00UW.

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. 2 hits.
HAMAPiMF_01617. FadJ. 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.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH_1. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
TIGRFAMsiTIGR02440. FadJ. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFADJ_VIBVY
AccessioniPrimary (citable) accession number: Q7MIS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 96 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

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.