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Q07ZP8 (FADJ_SHEFN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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:Sfri_2676
OrganismShewanella frigidimarina (strain NCIMB 400) [Complete proteome] [HAMAP]
Taxonomic identifier318167 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length710 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 – 710710Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000273984

Regions

Region1 – 190190Enoyl-CoA hydratase By similarity
Region310 – 7104013-hydroxyacyl-CoA dehydrogenase By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q07ZP8 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 7E9A39507BA4C8D3

FASTA71076,491
        10         20         30         40         50         60 
MSMEKTFNLA RRDDGIAILT MDVPGETMNT LKEQFGPEIS EILTEIKADS SIKGLVVISG 

        70         80         90        100        110        120 
KADSFVAGAD ITMLAACKNE EQAKTLSQQG HVVFAELEGL SIPVVAAING ACLGGGLELA 

       130        140        150        160        170        180 
LACHLRVCSD DKKTMLGVPE VQLGLLPGGG GTQRLPRLVG ITTALDMMLT GKQIRPKQAL 

       190        200        210        220        230        240 
KMGLVNDVVP NSILLETAVE LAKKGKQAAK PVVQSKINQF LESTSFTRDI IFDQARKQVL 

       250        260        270        280        290        300 
KKTQGNYPAP AKIIDCVRQG MNKGMVKGLE VEATHFANLV MSKESAALRS LFFATTEMKK 

       310        320        330        340        350        360 
ETGAEGAVPR KVKKVMVLGG GLMGGGIASV TTTKAKIPAR VKDISEQGLS NALSYAYKLL 

       370        380        390        400        410        420 
DKGVKRRHMT PIARDNIMAL MTTTTEYTGI KDADIVVEAV FEDLALKHKM VQDVERECGE 

       430        440        450        460        470        480 
NTIFASNTSS LPIGQIAAAA SRPENVIGLH YFSPVEKMPL VEVIAHKTTS PETIATTVAF 

       490        500        510        520        530        540 
ARKQGKTPIV VQDGAGFYVN RILALYMNEA AQLLLEGQRI EHLDRALVKF GFPVGPMTLL 

       550        560        570        580        590        600 
DEVGIDVGAK ISPILEKELG DRFKAPAAFD KLLADDRKGR KNGKGFYQYG PKAKKAKLVD 

       610        620        630        640        650        660 
ESVYKVLDIL IASDKEAKGV AERCTIQMLN EAVRCLEEGI IASARDGDIG AIFGIGFPPF 

       670        680        690        700        710 
LGGPFRYIDT LGASNLVATL QGYQSLYGDR FAPCDTLVKM ASDGSQFYKK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000447 Genomic DNA. Translation: ABI72516.1.
RefSeqYP_751355.1. NC_008345.1.

3D structure databases

ProteinModelPortalQ07ZP8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318167.Sfri_2676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI72516; ABI72516; Sfri_2676.
GeneID4279582.
KEGGsfr:Sfri_2676.
PATRIC23499439. VBISheFri14343_2777.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycSFRI318167:GIXS-2773-MONOMER.
UniPathwayUPA00659.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
HAMAPMF_01617. FadJ.
InterProIPR006176. 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.
IPR018376. Enoyl-CoA_hyd/isom_CS.
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.
SSF52096. SSF52096. 1 hit.
TIGRFAMsTIGR02440. FadJ. 1 hit.
PROSITEPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_SHEFN
AccessionPrimary (citable) accession number: Q07ZP8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 31, 2006
Last modified: June 11, 2014
This is version 57 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