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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
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

Pathway: 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)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

BioCyciECOL439855:GHHB-2498-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:EcSMS35_2500
OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
Taxonomic identifieri439855 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007011 Componenti: Chromosome

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 – 714714Fatty acid oxidation complex subunit alphaPRO_1000185944Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliB1LME7.
SMRiB1LME7. Positions 1-707.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydrataseUniRule annotationAdd
BLAST
Regioni306 – 7144093-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. 1 hit.
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.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1LME7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK
60 70 80 90 100
ELRGVVFVSA KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL
110 120 130 140 150
PVPVIAAIHG ACLGGGLELA LACHGRVCTD DAKTVLGLPE VQLGLLPGSG
160 170 180 190 200
GTQRLPRLIG VSTALEMILT GKQLRAKQAL KLGLVDDVVP QSILLEAAVE
210 220 230 240 250
LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT QGNYPATERI
260 270 280 290 300
LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDSG
310 320 330 340 350
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLSVRIKDI NPQGINHALK
360 370 380 390 400
YSWDQLEGKV RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL
410 420 430 440 450
ELKQQMVAEV EQNCATHTIF ASNTSSLPIG DIAAHAARPE QVIGLHFFSP
460 470 480 490 500
VEKMPLVEII PHASTSAQTI ATTVKLAKKQ GKTPIVVRDK AGFYVNRILA
510 520 530 540 550
PYINEAIRML TEGERIEHID AALVKFGFPV GPIQLLDEVG IDTGTKIIPV
560 570 580 590 600
LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
610 620 630 640 650
IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV
660 670 680 690 700
FGIGFPPFLG GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMSK
710
RGESFWKTTA TDLQ
Length:714
Mass (Da):77,074
Last modified:April 29, 2008 - v1
Checksum:i3B3600CF8971C888
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB18415.1.
RefSeqiWP_000425025.1. NC_010498.1.
YP_001744544.1. NC_010498.1.

Genome annotation databases

EnsemblBacteriaiACB18415; ACB18415; EcSMS35_2500.
KEGGiecm:EcSMS35_2500.
PATRICi18433898. VBIEscCol6161_2665.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000970 Genomic DNA. Translation: ACB18415.1.
RefSeqiWP_000425025.1. NC_010498.1.
YP_001744544.1. NC_010498.1.

3D structure databases

ProteinModelPortaliB1LME7.
SMRiB1LME7. Positions 1-707.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB18415; ACB18415; EcSMS35_2500.
KEGGiecm:EcSMS35_2500.
PATRICi18433898. VBIEscCol6161_2665.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciECOL439855:GHHB-2498-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
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.
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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
    Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
    J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SMS-3-5 / SECEC.

Entry informationi

Entry nameiFADJ_ECOSM
AccessioniPrimary (citable) accession number: B1LME7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: June 24, 2015
This is version 61 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.