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B0TL21 (FADJ_SHEHH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Shal_2670
OrganismShewanella halifaxensis (strain HAW-EB4) [Complete proteome] [HAMAP]
Taxonomic identifier458817 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length708 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 HAMAP-Rule MF_01617.

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.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid degradation
Lipid metabolism
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionIsomerase
Lyase
Oxidoreductase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

3-hydroxybutyryl-CoA epimerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

NAD binding

Inferred from electronic annotation. Source: InterPro

enoyl-CoA hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 708708Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_1000088063

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region310 – 7083993-hydroxyacyl-CoA dehydrogenase By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B0TL21 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: A0C731D06441039D

FASTA70876,230
        10         20         30         40         50         60 
MDMEKTFNLT RRDDGIAILT MDVPGETMNT LRSEFGPEIS DVLAEIKADT SIKGLVLVSG 

        70         80         90        100        110        120 
KKDSFVAGAD ISMLDACETA TDAKQLSQQG HVVFNELESL PIPVVAAING ACLGGGLELA 

       130        140        150        160        170        180 
LACHKRVCSL NPKTMMGVPE VQLGLLPGGG GTQRLPRLVG VTTALDMMLT GKQLRPKQAL 

       190        200        210        220        230        240 
KMGLVDDAVP ESILLRTAVE MALAGKRPAK KKHQSFFNKV LEGTSAGRNI IFDQAGKQVA 

       250        260        270        280        290        300 
KKTQGNYPAP AKIIDCVRQG MTKGMAKGLE VEASHFADLV MSKESGAMRS VFFATTEMKK 

       310        320        330        340        350        360 
ETGAGDVEPQ KVNKVMVLGG GLMGGGIASV TTTKAKIPAR VKDISETGLS NALAYAYKLL 

       370        380        390        400        410        420 
DKGVKRRHMT PAVRDNLMAL MTTTTEYKGI KDADIVVEAV FEDLALKHQM VKDVERECGE 

       430        440        450        460        470        480 
HTIFASNTSS LPIGQIAEAA SRPENVIGLH YFSPVEKMPL VEVIAHEKTS AETIATTVAF 

       490        500        510        520        530        540 
AKKQGKTPIV VQDGAGFYVN RILALYMNEA AQLLLEGQSV EHLDKALIKF GFPVGPMTLL 

       550        560        570        580        590        600 
DEVGIDVGAK ISPILEKELG ERFKAPTAFD KLLADDRKGR KNGKGFYLYG GKKKAKEVDQ 

       610        620        630        640        650        660 
TVYSVLGLKP GVDTEATEVA QRCVVQMLNE AVRCLEESII ACPRDGDIGA IFGIGFPPFL 

       670        680        690        700 
GGPFHYIDTL GAANLVKILE NYQSRYGSRF EPAAKLKQMA EEGTRFFS 

« Hide

References

[1]"Complete sequence of Shewanella halifaxensis HAW-EB4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Zhao J.-S., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HAW-EB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000931 Genomic DNA. Translation: ABZ77223.1.
RefSeqYP_001674882.1. NC_010334.1.

3D structure databases

ProteinModelPortalB0TL21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING458817.Shal_2670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ77223; ABZ77223; Shal_2670.
GeneID5902951.
KEGGshl:Shal_2670.
PATRIC23508199. VBISheHal24697_2810.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAMMLNEAA.
OrthoDBEOG6M9F0M.
ProtClustDBPRK11154.

Enzyme and pathway databases

BioCycSHAL458817:GH1X-2766-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
HAMAPMF_01617. FadJ.
InterProIPR006176. 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. SSF48179. 2 hits.
TIGRFAMsTIGR02440. FadJ. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFADJ_SHEHH
AccessionPrimary (citable) accession number: B0TL21
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways