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Q7N288 (FADJ_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. 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:plu3200
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus ›

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.

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 caution

The sequence CAE15574.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 727727Fatty acid oxidation complex subunit alpha HAMAP-Rule MF_01617
PRO_0000109303

Regions

Region16 – 205190Enoyl-CoA hydratase By similarity
Region321 – 7274073-hydroxyacyl-CoA dehydrogenase By similarity

Sites

Site1331Important for catalytic activity By similarity
Site1551Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N288 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 5173D0EE51FB2930

FASTA72779,265
        10         20         30         40         50         60 
MTQAQHDAAP ITTGTNQTAS VFSFDVRPDK IGIITINVPG EKVNTLKAEF VDQFLNVFKQ 

        70         80         90        100        110        120 
AQQSSGLKGL ILISGKPDTF IAGADISMIA GCKTKEDARD LAEKGQKLFS QIANYPLPVV 

       130        140        150        160        170        180 
AAIHGACLGG GLELALACHW RVCSQDDKTR LGLPEVQLGL LPGSGGTQRL PRLIGVSSAL 

       190        200        210        220        230        240 
DIMLTGKQLR AKQALRLGLV DDAVPLDILL DIAIEKVKKG IPVRKPLPWQ QRLLVGPVGR 

       250        260        270        280        290        300 
YFLFNIVRKK TLAKTRGHYP APERIIEVVK EGLEKGMSQG LRAEAVAFGE LAMTRESAAL 

       310        320        330        340        350        360 
RNLFFAATSL KNETGSSEKP AKIKHVGILG GGLMGGGIAN VTATRGKLPV RIKDINEKGI 

       370        380        390        400        410        420 
SQVLKYTWDL LSKRVKQKRL RPAERAQQMM LISGTTDYRG FAQTDIVVEA VFEDLSLKQK 

       430        440        450        460        470        480 
MVAEIETNAK PETIFASNTS SLPIHQIAEK AQRPEQVIGL HYFSPVDKMP LVEVIPHQGT 

       490        500        510        520        530        540 
SEKTIATAVS LAKKQGKTAI VVGDKAGFYV NRILVPYISE AAHCLVAGEP IDHIDGALVN 

       550        560        570        580        590        600 
FGFPVGPINL LDEVGIDVGT KIMPVLVEQL GPRFAAPESL DAVLKDGRKG RKNGRGFYLY 

       610        620        630        640        650        660 
APGPRKFWQF GKRDKKVDSS VYTLLNITPE SHMLSSEIAQ RCVMLMLNEA VRCLDEGIIR 

       670        680        690        700        710        720 
SPRDGDIGAV FGIGFPPFFG GPFRYIDSLG CARVVEILRR LESQYGDRFV PCECLVNMAE 


QNKSFYP

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References

[1]"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens."
Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K. expand/collapse author list , Siguier P., Vincent R., Wingate V., Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.
Nat. Biotechnol. 21:1307-1313(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TT01.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX571869 Genomic DNA. Translation: CAE15574.1. Different initiation.
RefSeqNP_930429.2. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N288.
ModBaseSearch...

Protein-protein interaction databases

STRING243265.plu3200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE15574; CAE15574; plu3200.
GeneID2803211.
KEGGplu:plu3200.
PATRIC20510816. VBIPhoLum48522_3649.

Organism-specific databases

GenoListplu3200.
CMRSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261346.
KOK01782.
ProtClustDBPRK11154.

Enzyme and pathway databases

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_PHOLL
AccessionPrimary (citable) accession number: Q7N288
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 76 of the entry and version 2 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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