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Protein

Peroxisomal bifunctional enzyme

Gene

ehhadh

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

(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:ifatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001Substrate; via amide nitrogenBy similarity
Sitei123 – 1231Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal bifunctional enzyme
Short name:
PBE
Short name:
PBFE
Including the following 2 domains:
Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.17, EC:5.3.3.8)
3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:ehhadh
Synonyms:echd
ORF Names:si:dkeyp-30d5.2, zgc:77526
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 9

Organism-specific databases

ZFINiZDB-GENE-040426-2581. ehhadh.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 718717Peroxisomal bifunctional enzymePRO_0000353182Add
BLAST

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

BgeeiQ6NYL3.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi7955.ENSDARP00000093211.

Structurei

3D structure databases

ProteinModelPortaliQ6NYL3.
SMRiQ6NYL3. Positions 260-709.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 280279Enoyl-CoA hydratase / isomeraseAdd
BLAST
Regioni281 – 5672873-hydroxyacyl-CoA dehydrogenaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi716 – 7183Microbody targeting signalBy similarity

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ6NYL3.
KOiK07514.
OMAiFGYGFPR.
OrthoDBiEOG725DH0.
PhylomeDBiQ6NYL3.
TreeFamiTF316708.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6NYL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARYELVKRS VALITLTNPP VNALSSAVRH AISKTMERAL SDPKVTAVVI
60 70 80 90 100
CGENGRFCGG ADIREFAGPL RGPPLVPLLD AIEAGEKPVV AAIEGVALGG
110 120 130 140 150
GFELALVCHY RIAHYKARLG LPEVTLGILP AAGGTQRLPR LIGIPAALEL
160 170 180 190 200
ITTGRHVSAQ EALKLGMVDQ VTEQNTCEVA LEFALKAVGK PLSSRRLSML
210 220 230 240 250
TTPCPPGLDG IFEAATMQVQ KKARGVMAPL ACVQAVRAAT LPYSEGIKRE
260 270 280 290 300
GELMATLFSS GQAQALQYSF FAQRTAEKWT LPSGAQWNNS KPREIQSAAV
310 320 330 340 350
IGLGTMGRGI VVSLARVGIS VIAVESEKKL LETGRQMVIG MLERDAKRRG
360 370 380 390 400
VSASLNLLKF SLSLQDLKDV DLVIEAVFED MALKKQIFRE LSRVCRPATL
410 420 430 440 450
LCSNTSGLDV DALADVTDRP QLVAGMHFFS PAHVMKLLEV VCGPRSSKEA
460 470 480 490 500
IATAMSLGKR MGKVSVAVGN CPGFVGNRML MPYLEQATFL LEEGATPQQI
510 520 530 540 550
DKALEDFGFA MGVFRMSDLA GLDVGWRVRK ESGLTGPDVD PKDPPRRRQG
560 570 580 590 600
RKYCPIPDMV CQQGRFGQKT GRGWYMYDKP GDTNAKPDPL IQNLLETYRS
610 620 630 640 650
RYGIQPRKIT DQEIIERCLF ALANEGFRIL KDKIAGQPED IDVIYLFGYG
660 670 680 690 700
FPRHRGGPMF YASMVGLERV LERLEYYHHA LPDVPHLEPS PLLKKLVARG
710
SPPIQKWREH IKSMHSHL
Length:718
Mass (Da):78,508
Last modified:July 5, 2004 - v1
Checksum:iEA4DC2FDDCAE95B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR936497 Genomic DNA. Translation: CAP19438.1.
BC066545 mRNA. Translation: AAH66545.1.
RefSeqiNP_996951.1. NM_207068.1.
UniGeneiDr.80045.

Genome annotation databases

EnsembliENSDART00000102434; ENSDARP00000093211; ENSDARG00000070029.
GeneIDi100000859.
KEGGidre:100000859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR936497 Genomic DNA. Translation: CAP19438.1.
BC066545 mRNA. Translation: AAH66545.1.
RefSeqiNP_996951.1. NM_207068.1.
UniGeneiDr.80045.

3D structure databases

ProteinModelPortaliQ6NYL3.
SMRiQ6NYL3. Positions 260-709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000093211.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000102434; ENSDARP00000093211; ENSDARG00000070029.
GeneIDi100000859.
KEGGidre:100000859.

Organism-specific databases

CTDi1962.
ZFINiZDB-GENE-040426-2581. ehhadh.

Phylogenomic databases

eggNOGiCOG1250.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ6NYL3.
KOiK07514.
OMAiFGYGFPR.
OrthoDBiEOG725DH0.
PhylomeDBiQ6NYL3.
TreeFamiTF316708.

Enzyme and pathway databases

UniPathwayiUPA00659.

Miscellaneous databases

NextBioi20784820.
PROiQ6NYL3.

Gene expression databases

BgeeiQ6NYL3.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiECHP_DANRE
AccessioniPrimary (citable) accession number: Q6NYL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: July 5, 2004
Last modified: July 22, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.