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C6DAL7 (FADJ_PECCP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 36. 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:PC1_2821
OrganismPectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]
Taxonomic identifier561230 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length727 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 – 727727Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_1000215731

Regions

Region1 – 200200Enoyl-CoA hydratase By similarity
Region316 – 7274123-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1281Important for catalytic activity By similarity
Site1501Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
C6DAL7 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: A1443F5E2F6E66F5

FASTA72779,712
        10         20         30         40         50         60 
MNDQQPFSAI TESPSAFSLT IRPDNIGVIG IDVPGEKVNT LKSEFAQQIL SVFEQARQHA 

        70         80         90        100        110        120 
TLRGLILISS KPDSFIAGAD ITMLNQCRSA EQAENLAKQG QETFEQIAAL PFPVVAAIHG 

       130        140        150        160        170        180 
ACLGGGLELA LACDYRVCSL DEKTVLGLPE VQLGLLPGSG GTQRLPRLIG LDSALDLILT 

       190        200        210        220        230        240 
GRHLRANQAL RQGLVDEAVP HDILLDTAVE MLKKGKRKAE PLGWRSRLLS SPGIRHVLFK 

       250        260        270        280        290        300 
MVKRKTRAKT HGNYPATEKI IQVVRRGVEK GREEGYRQEA RAFGKLVMTP ESAALRHLFF 

       310        320        330        340        350        360 
ASNALKKTSG AASDAKPIHY VGILGGGLMG GGIASVTATR GQLPVRIKDI NEQGINHALK 

       370        380        390        400        410        420 
YNWQLLTQRV QRKRMKPTER QRLMTLISGS TDYRGFEHAD IVIEAVFEDL ALKRQMVAEI 

       430        440        450        460        470        480 
EDHAAPHTIF ASNTSSLPIH QIAEGARRPQ QVIGLHYFSP VDKMPLVEVI PHAHTSAETV 

       490        500        510        520        530        540 
ATTVALARKQ GKTAIVVGDS AGFYVNRILA PYINEAAYCL LEGEPIESID YALVRFGFPV 

       550        560        570        580        590        600 
GPFALLDEVG IDVATKIVPV LSEELGTRFT SPPAFDAILK DGRKGRKNGK GFYRYNKTRR 

       610        620        630        640        650        660 
FWQTGREVDS SIYPLLDVTA KAHIDPALIS QRGVMMMLNE AARCLDEGVI QCARDGDIGA 

       670        680        690        700        710        720 
VFGIGFPPFL GGPFHYMDRL GMETVVKTLL VLQQQYGDRF APCERLLAMR EGQRTFYPPT 


DEDDSAS 

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References

[1]"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001657 Genomic DNA. Translation: ACT13851.1.
RefSeqYP_003018387.1. NC_012917.1.

3D structure databases

ProteinModelPortalC6DAL7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561230.PC1_2821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT13851; ACT13851; PC1_2821.
GeneID8133774.
KEGGpct:PC1_2821.
PATRIC20490334. VBIPecCar70489_2844.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
OMAPFRYMDT.
OrthoDBEOG6M9F0M.

Enzyme and pathway databases

BioCycPCAR561230:GKCK-2875-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.
InterProIPR006180. 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.
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.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFADJ_PECCP
AccessionPrimary (citable) accession number: C6DAL7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: June 11, 2014
This is version 36 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