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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids.2 Publications

Catalytic activityi

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

Pathway:ifatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
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 activityBy similarity
Sitei140 – 1401Important for catalytic activityBy similarity

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

BioCyciEcoCyc:G7212-MONOMER.
ECOL316407:JW2338-MONOMER.
MetaCyc:G7212-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alpha
Including the following 2 domains:
Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase (EC:4.2.1.17, EC:5.1.2.3)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadJ
Synonyms:yfcX
Ordered Locus Names:b2341, JW2338
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14127. fadJ.

Subcellular locationi

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_0000109298Add
BLAST

Expressioni

Inductioni

Unlike the aerobic pathway, the anaerobic pathway is not strongly repressed by FadR regulatory protein.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI).By similarity

Protein-protein interaction databases

DIPiDIP-11990N.
IntActiP77399. 8 interactions.
STRINGi511145.b2341.

Structurei

3D structure databases

ProteinModelPortaliP77399.
SMRiP77399. Positions 6-706.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydrataseAdd
BLAST
Regioni306 – 7144093-hydroxyacyl-CoA dehydrogenaseAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
InParanoidiP77399.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.
PhylomeDBiP77399.

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.

P77399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMTSAFTLN VRLDNIAVIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK
60 70 80 90 100
ELRGVVFVSA KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL
110 120 130 140 150
PIQVIAAIHG ACLGGGLELA LACHGRVCTD DPKTVLGLPE VQLGLLPGSG
160 170 180 190 200
GTQRLPRLIG VSTALEMILT GKQLRAKQAL KLGLVDDVVP HSILLEAAVE
210 220 230 240 250
LAKKERPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT QGNYPATERI
260 270 280 290 300
LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTDVKKDPG
310 320 330 340 350
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGIPVRIKDI NPQGINHALK
360 370 380 390 400
YSWDQLEGKV RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL
410 420 430 440 450
ELKQQMVAEV EQNCAAHTIF ASNTSSLPIG DIAAHATRPE QVIGLHFFSP
460 470 480 490 500
VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ GKTPIVVRDK AGFYVNRILA
510 520 530 540 550
PYINEAIRML TQGERVEHID AALVKFGFPV GPIQLLDEVG IDTGTKIIPV
560 570 580 590 600
LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
610 620 630 640 650
IYPLIGTQGQ GRISAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV
660 670 680 690 700
FGIGFPPFLG GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMGA
710
RGESFWKTTA TDLQ
Length:714
Mass (Da):77,072
Last modified:February 1, 1997 - v1
Checksum:iF4E0A75680039A0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75401.1.
AP009048 Genomic DNA. Translation: BAA16195.1.
PIRiC65007.
RefSeqiNP_416843.1. NC_000913.3.
WP_000426176.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC75401; AAC75401; b2341.
BAA16195; BAA16195; BAA16195.
GeneIDi949097.
KEGGieco:b2341.
PATRICi32120055. VBIEscCol129921_2437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75401.1.
AP009048 Genomic DNA. Translation: BAA16195.1.
PIRiC65007.
RefSeqiNP_416843.1. NC_000913.3.
WP_000426176.1. NZ_CP010445.1.

3D structure databases

ProteinModelPortaliP77399.
SMRiP77399. Positions 6-706.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-11990N.
IntActiP77399. 8 interactions.
STRINGi511145.b2341.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75401; AAC75401; b2341.
BAA16195; BAA16195; BAA16195.
GeneIDi949097.
KEGGieco:b2341.
PATRICi32120055. VBIEscCol129921_2437.

Organism-specific databases

EchoBASEiEB3879.
EcoGeneiEG14127. fadJ.

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261346.
InParanoidiP77399.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.
PhylomeDBiP77399.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciEcoCyc:G7212-MONOMER.
ECOL316407:JW2338-MONOMER.
MetaCyc:G7212-MONOMER.

Miscellaneous databases

PROiP77399.

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

« Hide 'large scale' publications
  1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains."
    Snell K.D., Feng F., Zhong L., Martin D., Madison L.L.
    J. Bacteriol. 184:5696-5705(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway."
    Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.
    Mol. Microbiol. 47:793-805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiFADJ_ECOLI
AccessioniPrimary (citable) accession number: P77399
Secondary accession number(s): Q6KCX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: July 22, 2015
This is version 137 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.