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B1LME7 (FADJ_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fatty acid oxidation complex subunit alpha

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase
    EC=4.2.1.17
    EC=5.1.2.3
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:fadJ
Ordered Locus Names:EcSMS35_2500
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01617

Catalytic activity

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O. HAMAP-Rule MF_01617

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH. HAMAP-Rule MF_01617

(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA. HAMAP-Rule MF_01617

Pathway

Lipid metabolism; fatty acid beta-oxidation. HAMAP-Rule MF_01617

Subunit structure

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 714714Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_1000185944

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region306 – 7144093-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1181Important for catalytic activity By similarity
Site1401Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LME7 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 3B3600CF8971C888

FASTA71477,074
        10         20         30         40         50         60 
MEMASAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA 

        70         80         90        100        110        120 
KPDNFIAGAD INMIGNCKTA QEAEVLARQG QQLMAEIHAL PVPVIAAIHG ACLGGGLELA 

       130        140        150        160        170        180 
LACHGRVCTD DAKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL 

       190        200        210        220        230        240 
KLGLVDDVVP QSILLEAAVE LAKQDRPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT 

       250        260        270        280        290        300 
QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRNIFF ASTEVKKDSG 

       310        320        330        340        350        360 
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGLSVRIKDI NPQGINHALK YSWDQLEGKV 

       370        380        390        400        410        420 
RRRHLKASER DKQLALISGT TDYCGFAHRD LIIEAVFENL ELKQQMVAEV EQNCATHTIF 

       430        440        450        460        470        480 
ASNTSSLPIG DIAAHAARPE QVIGLHFFSP VEKMPLVEII PHASTSAQTI ATTVKLAKKQ 

       490        500        510        520        530        540 
GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERIEHID AALVKFGFPV GPIQLLDEVG 

       550        560        570        580        590        600 
IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 

       610        620        630        640        650        660 
IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCLDEQVIR SVRDGDIGAV FGIGFPPFLG 

       670        680        690        700        710 
GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMSK RGESFWKTTA TDLQ

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000970 Genomic DNA. Translation: ACB18415.1.
RefSeqYP_001744544.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LME7.
SMRB1LME7. Positions 1-707.
ModBaseSearch...

Protein-protein interaction databases

STRING439855.EcSMS35_2500.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB18415; ACB18415; EcSMS35_2500.
GeneID6146373.
KEGGecm:EcSMS35_2500.
PATRIC18433898. VBIEscCol6161_2665.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMASPKRDKG.
ProtClustDBPRK11154.

Enzyme and pathway databases

BioCycECOL439855:GHHB-2989-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01617. FadJ.
InterProIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR012802. FadJ.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. 6DGDH_C_like. 2 hits.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_ECOSM
AccessionPrimary (citable) accession number: B1LME7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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