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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Escherichia coli O1:K1 / APEC
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

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP
  4. NAD binding Source: InterPro

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

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:Ecok1_22340
ORF Names:APECO1_4225
OrganismiEscherichia coli O1:K1 / APEC
Taxonomic identifieri405955 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008216 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 714714Fatty acid oxidation complex subunit alphaPRO_1000069485Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi405955.APECO1_4225.

Structurei

3D structure databases

ProteinModelPortaliA1ADI8.
SMRiA1ADI8. 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.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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.

A1ADI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQIRENK
60 70 80 90 100
ELRGVVFVSA KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL
110 120 130 140 150
PIPVIAAIHG ACLGGGLELA LACHGRVCTD DPKTVLGLPE VQLGLLPGSG
160 170 180 190 200
GTQRLPRLIG VSTALEMILT GKQLRAKQAV KLGLVDDVVP HSILLEAAVE
210 220 230 240 250
LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT QGNYPATERI
260 270 280 290 300
LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTDVKKDPG
310 320 330 340 350
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLPVRIKDI NPRGINHALK
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 IDTGTKIMPV
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 PCDRLVEMSE
710
RGESFWKTTA TDLQ
Length:714
Mass (Da):77,148
Last modified:January 22, 2007 - v1
Checksum:iD05212AF62C80111
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABJ01728.1.
RefSeqiYP_853442.1. NC_008563.1.

Genome annotation databases

EnsemblBacteriaiABJ01728; ABJ01728; APECO1_4225.
KEGGiecv:APECO1_4225.
PATRICi18216607. VBIEscCol127180_2565.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000468 Genomic DNA. Translation: ABJ01728.1.
RefSeqiYP_853442.1. NC_008563.1.

3D structure databases

ProteinModelPortaliA1ADI8.
SMRiA1ADI8. Positions 1-707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi405955.APECO1_4225.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABJ01728; ABJ01728; APECO1_4225.
KEGGiecv:APECO1_4225.
PATRICi18216607. VBIEscCol127180_2565.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

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. 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.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
    Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
    J. Bacteriol. 189:3228-3236(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiFADJ_ECOK1
AccessioniPrimary (citable) accession number: A1ADI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 4, 2008
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 66 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.