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Protein

Peroxisomal bifunctional enzyme

Gene

EHHADH

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalytic activityi

(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Enzyme regulationi

Enzyme activity enhanced by acetylation.By similarity

Pathwayi: fatty 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)DescriptionActionsGraphical viewLength
Binding sitei103Substrate; via amide nitrogenBy similarity1
Sitei106Important for catalytic activityBy similarity1
Sitei126Important for catalytic activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid metabolism, Lipid metabolism
LigandNAD

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricomorphaCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001092461 – 726Peroxisomal bifunctional enzymeAdd BLAST726

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei167N6-acetyllysine; alternateBy similarity1
Modified residuei167N6-succinyllysine; alternateBy similarity1
Modified residuei173N6-acetyllysineBy similarity1
Modified residuei185N6-succinyllysineBy similarity1
Modified residuei221N6-acetyllysine; alternateBy similarity1
Modified residuei221N6-succinyllysine; alternateBy similarity1
Modified residuei282N6-succinyllysineBy similarity1
Modified residuei292N6-succinyllysineBy similarity1
Modified residuei333N6-succinyllysineBy similarity1
Modified residuei348N6-acetyllysineBy similarity1
Modified residuei352N6-acetyllysineBy similarity1
Modified residuei467N6-acetyllysineBy similarity1
Modified residuei535N6-succinyllysineBy similarity1
Modified residuei587N6-acetyllysine; alternateBy similarity1
Modified residuei587N6-succinyllysine; alternateBy similarity1
Modified residuei594N6-acetyllysine; alternateBy similarity1
Modified residuei594N6-succinyllysine; alternateBy similarity1
Modified residuei713N6-acetyllysine; alternateBy similarity1
Modified residuei713N6-succinyllysine; alternateBy similarity1
Modified residuei725N6-succinyllysineBy similarity1

Post-translational modificationi

Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TCA) or with nicotinamide (NAM) with highest increase on Lys-348. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP55100

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000019312

Structurei

3D structure databases

ProteinModelPortaliP55100
SMRiP55100
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 284Enoyl-CoA hydratase / isomeraseAdd BLAST284
Regioni285 – 5753-hydroxyacyl-CoA dehydrogenaseAdd BLAST291

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi724 – 726Microbody targeting signalBy similarity3

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

eggNOGiKOG1683 Eukaryota
COG1250 LUCA
HOGENOMiHOG000261347
HOVERGENiHBG104990
InParanoidiP55100

Family and domain databases

InterProiView protein in InterPro
IPR006176 3-OHacyl-CoA_DH_NAD-bd
IPR006108 3HC_DH_C
IPR008927 6-PGluconate_DH-like_C_sf
IPR029045 ClpP/crotonase-like_dom_sf
IPR018376 Enoyl-CoA_hyd/isom_CS
IPR001753 Enoyl-CoA_hydra/iso
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00725 3HCDH, 2 hits
PF02737 3HCDH_N, 1 hit
PF00378 ECH_1, 1 hit
SUPFAMiSSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
SSF52096 SSF52096, 1 hit
PROSITEiView protein in PROSITE
PS00166 ENOYL_COA_HYDRATASE, 1 hit

Sequencei

Sequence statusi: Complete.

P55100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYLRLPHS LALIRLRNPP VNAISPAVIH GIKEGLQKAM SDYTIKGIVI
60 70 80 90 100
SGANNIFCAG ADIHGFSAPL SFGTGSGLGP IVDEMQRYEK PVVAAIQGMA
110 120 130 140 150
LGGGLELSLG CHYRIAHAEA RIGFPEVTLG ILPGARGTQL LPRLIGVPAA
160 170 180 190 200
LDLITSGRHI TAGEALKLGI LDKVVNSAPV EEAIKFAQKI LNQPLEPRRI
210 220 230 240 250
LNRPVSSLPN MDAIFGEAVE KMRRQHPGQL APETCVRSVQ ASVQYPYEGG
260 270 280 290 300
IMKERELFLN LQHSGQAKAL QYAFFAERSA PKWSTPSGAS WKTAAARPVS
310 320 330 340 350
SVGVLGLGTM GRGIAISFAR VGIPVIAVES DPKQLETAQK LITSILEKEA
360 370 380 390 400
SKSRQQCGQQ RSGPKPRFSS SMKDLASVDL VVEAVFEDMN LKKRVFAELS
410 420 430 440 450
AVCKPEAFLC TNTSALDVDE IATSTNRPQQ VIGTHFFSPA HVMKLLEVIP
460 470 480 490 500
SRHSSPTTIA TVMDLAKKIK KVAVVVGNCY GFVGNRMLRS YYEQTNFLLE
510 520 530 540 550
DGSKPEDIDQ ALEEFGFRMG PFRVSDLAGL DVGWKIRKGQ GLTGPSLQGT
560 570 580 590 600
APARKRGNAR YSPIADMLCE LGRFGQKTGQ GWYKYDKPLG RIHKPDPWLS
610 620 630 640 650
KFLSEYRETH HIKPRVIGRD EILERCLYAL INEAFRILGE GIAASPEHID
660 670 680 690 700
VIYLHGYGWP RHKGGPMFYA ASVGLPTVLE KLQKYYQQNP DIPHLEPCNY
710 720
LKKLASQGNP PLKEWQSLAG LPSSKL
Length:726
Mass (Da):79,375
Last modified:January 23, 2007 - v2
Checksum:iF1702122D62C5FF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92742 mRNA Translation: CAA63403.1
X85112 mRNA Translation: CAA59431.1
PIRiS68697 S57651
RefSeqiNP_001166417.1, NM_001172946.1

Genome annotation databases

GeneIDi100135519

Similar proteinsi

Entry informationi

Entry nameiECHP_CAVPO
AccessioniPrimary (citable) accession number: P55100
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 124 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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