Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6NYL3 (ECHP_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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:
Peroxisomal bifunctional enzyme

Short name=PBE
Short name=PBFE

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
    EC=4.2.1.17
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:ehhadh
Synonyms:echd
ORF Names:si:dkeyp-30d5.2, zgc:77526
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

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

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

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

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 718717Peroxisomal bifunctional enzyme
PRO_0000353182

Regions

Region2 – 280279Enoyl-CoA hydratase / isomerase
Region281 – 5672873-hydroxyacyl-CoA dehydrogenase
Motif716 – 7183Microbody targeting signal By similarity

Sites

Binding site1001Substrate; via amide nitrogen By similarity
Site1231Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NYL3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EA4DC2FDDCAE95B1

FASTA71878,508
        10         20         30         40         50         60 
MARYELVKRS VALITLTNPP VNALSSAVRH AISKTMERAL SDPKVTAVVI CGENGRFCGG 

        70         80         90        100        110        120 
ADIREFAGPL RGPPLVPLLD AIEAGEKPVV AAIEGVALGG GFELALVCHY RIAHYKARLG 

       130        140        150        160        170        180 
LPEVTLGILP AAGGTQRLPR LIGIPAALEL ITTGRHVSAQ EALKLGMVDQ VTEQNTCEVA 

       190        200        210        220        230        240 
LEFALKAVGK PLSSRRLSML TTPCPPGLDG IFEAATMQVQ KKARGVMAPL ACVQAVRAAT 

       250        260        270        280        290        300 
LPYSEGIKRE GELMATLFSS GQAQALQYSF FAQRTAEKWT LPSGAQWNNS KPREIQSAAV 

       310        320        330        340        350        360 
IGLGTMGRGI VVSLARVGIS VIAVESEKKL LETGRQMVIG MLERDAKRRG VSASLNLLKF 

       370        380        390        400        410        420 
SLSLQDLKDV DLVIEAVFED MALKKQIFRE LSRVCRPATL LCSNTSGLDV DALADVTDRP 

       430        440        450        460        470        480 
QLVAGMHFFS PAHVMKLLEV VCGPRSSKEA IATAMSLGKR MGKVSVAVGN CPGFVGNRML 

       490        500        510        520        530        540 
MPYLEQATFL LEEGATPQQI DKALEDFGFA MGVFRMSDLA GLDVGWRVRK ESGLTGPDVD 

       550        560        570        580        590        600 
PKDPPRRRQG RKYCPIPDMV CQQGRFGQKT GRGWYMYDKP GDTNAKPDPL IQNLLETYRS 

       610        620        630        640        650        660 
RYGIQPRKIT DQEIIERCLF ALANEGFRIL KDKIAGQPED IDVIYLFGYG FPRHRGGPMF 

       670        680        690        700        710 
YASMVGLERV LERLEYYHHA LPDVPHLEPS PLLKKLVARG SPPIQKWREH IKSMHSHL 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936497 Genomic DNA. Translation: CAP19438.1.
BC066545 mRNA. Translation: AAH66545.1.
RefSeqNP_996951.1. NM_207068.1.
UniGeneDr.80045.

3D structure databases

ProteinModelPortalQ6NYL3.
SMRQ6NYL3. Positions 260-709.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000093211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000102434; ENSDARP00000093211; ENSDARG00000070029.
GeneID100000859.
KEGGdre:100000859.

Organism-specific databases

CTD1962.
ZFINZDB-GENE-040426-2581. ehhadh.

Phylogenomic databases

eggNOGCOG1250.
GeneTreeENSGT00720000108673.
HOGENOMHOG000261347.
HOVERGENHBG104990.
InParanoidQ6NYL3.
KOK07514.
OMAGYGWPVY.
OrthoDBEOG725DH0.
PhylomeDBQ6NYL3.
TreeFamTF316708.

Enzyme and pathway databases

UniPathwayUPA00659.

Gene expression databases

BgeeQ6NYL3.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
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.
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.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20784820.
PROQ6NYL3.

Entry information

Entry nameECHP_DANRE
AccessionPrimary (citable) accession number: Q6NYL3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways