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Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.

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 sitei100Substrate; via amide nitrogenBy similarity1
Sitei103Important for catalytic activityBy similarity1
Sitei123Important for catalytic activityBy similarity1

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: RGD
  • dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
  • enoyl-CoA hydratase activity Source: UniProtKB-EC
  • enzyme binding Source: UniProtKB

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

BRENDAi4.2.1.17. 5301.
ReactomeiR-RNO-390918. Peroxisomal lipid metabolism.
SABIO-RKP07896.
UniPathwayiUPA00659.

Chemistry databases

SwissLipidsiSLP:000001144.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi621441. Ehhadh.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • mitochondrion Source: Ensembl
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001092491 – 722Peroxisomal bifunctional enzymeAdd BLAST722

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Blocked amino end (Ala)1
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei173N6-acetyllysine; alternateBy similarity1
Modified residuei173N6-succinyllysine; alternateBy similarity1
Modified residuei182N6-succinyllysineBy similarity1
Modified residuei190N6-acetyllysine; alternateBy similarity1
Modified residuei190N6-succinyllysine; alternateBy similarity1
Modified residuei218N6-acetyllysine; alternateBy similarity1
Modified residuei218N6-succinyllysine; alternateBy similarity1
Modified residuei241N6-succinyllysineBy similarity1
Modified residuei249N6-acetyllysineBy similarity1
Modified residuei253N6-succinyllysineBy similarity1
Modified residuei275N6-acetyllysine; alternateBy similarity1
Modified residuei275N6-succinyllysine; alternateBy similarity1
Modified residuei279N6-succinyllysineBy similarity1
Modified residuei289N6-succinyllysineBy similarity1
Modified residuei330N6-succinyllysineBy similarity1
Modified residuei345N6-acetyllysineBy similarity1
Modified residuei359N6-acetyllysineBy similarity1
Modified residuei463N6-acetyllysineBy similarity1
Modified residuei531N6-succinyllysineBy similarity1
Modified residuei547PhosphothreonineBy similarity1
Modified residuei576N6-succinyllysineBy similarity1
Modified residuei583N6-acetyllysine; alternateBy similarity1
Modified residuei583N6-succinyllysine; alternateBy similarity1
Modified residuei590N6-acetyllysine; alternateBy similarity1
Modified residuei590N6-succinyllysine; alternateBy similarity1
Modified residuei709N6-acetyllysine; alternateBy similarity1
Modified residuei709N6-succinyllysine; alternateBy similarity1
Modified residuei721N6-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-345. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP07896.
PRIDEiP07896.

PTM databases

iPTMnetiP07896.
PhosphoSitePlusiP07896.

Expressioni

Gene expression databases

BgeeiENSRNOG00000001770.
GenevisibleiP07896. RN.

Interactioni

Subunit structurei

Monomer.1 Publication

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

IntActiP07896. 6 interactors.
STRINGi10116.ENSRNOP00000002410.

Structurei

Secondary structure

1722
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Turni8 – 10Combined sources3
Beta strandi11 – 16Combined sources6
Turni19 – 22Combined sources4
Helixi26 – 40Combined sources15
Beta strandi47 – 53Combined sources7
Beta strandi63 – 65Combined sources3
Beta strandi67 – 69Combined sources3
Helixi74 – 84Combined sources11
Beta strandi89 – 93Combined sources5
Beta strandi95 – 98Combined sources4
Helixi100 – 106Combined sources7
Beta strandi108 – 114Combined sources7
Beta strandi118 – 120Combined sources3
Helixi122 – 126Combined sources5
Turni131 – 133Combined sources3
Helixi134 – 142Combined sources9
Helixi144 – 153Combined sources10
Beta strandi156 – 158Combined sources3
Helixi159 – 164Combined sources6
Beta strandi169 – 174Combined sources6
Helixi176 – 187Combined sources12
Beta strandi188 – 190Combined sources3
Helixi193 – 195Combined sources3
Helixi197 – 199Combined sources3
Helixi208 – 222Combined sources15
Helixi227 – 241Combined sources15
Helixi244 – 259Combined sources16
Helixi262 – 272Combined sources11
Helixi273 – 278Combined sources6
Beta strandi283 – 285Combined sources3
Turni288 – 290Combined sources3
Beta strandi298 – 302Combined sources5
Helixi306 – 316Combined sources11
Turni317 – 319Combined sources3
Beta strandi321 – 325Combined sources5
Helixi329 – 352Combined sources24
Beta strandi353 – 355Combined sources3
Beta strandi362 – 366Combined sources5
Helixi368 – 371Combined sources4
Beta strandi375 – 379Combined sources5
Helixi385 – 398Combined sources14
Beta strandi404 – 407Combined sources4
Beta strandi410 – 412Combined sources3
Helixi414 – 418Combined sources5
Helixi424 – 426Combined sources3
Beta strandi427 – 432Combined sources6
Turni436 – 438Combined sources3
Beta strandi441 – 446Combined sources6
Helixi452 – 464Combined sources13
Beta strandi468 – 472Combined sources5
Turni476 – 479Combined sources4
Helixi480 – 496Combined sources17
Helixi501 – 511Combined sources11
Helixi517 – 524Combined sources8
Helixi526 – 535Combined sources10
Beta strandi538 – 541Combined sources4
Helixi560 – 566Combined sources7
Turni572 – 575Combined sources4
Beta strandi576 – 583Combined sources8
Beta strandi589 – 591Combined sources3
Helixi593 – 605Combined sources13
Helixi615 – 635Combined sources21
Beta strandi638 – 640Combined sources3
Helixi642 – 652Combined sources11
Helixi657 – 659Combined sources3
Helixi662 – 669Combined sources8
Helixi671 – 684Combined sources14
Helixi689 – 691Combined sources3
Helixi695 – 702Combined sources8
Helixi708 – 710Combined sources3
Helixi711 – 715Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZCJX-ray1.90A260-722[»]
2X58X-ray2.80A/B1-722[»]
3ZW8X-ray2.50A/B1-722[»]
3ZW9X-ray2.90A/B1-722[»]
3ZWAX-ray2.47A/B1-722[»]
3ZWBX-ray3.10A/B1-722[»]
3ZWCX-ray2.30A/B1-722[»]
5AAJX-ray2.49A/B1-722[»]
5AAKX-ray2.80A/B1-722[»]
ProteinModelPortaliP07896.
SMRiP07896.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07896.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 281Enoyl-CoA hydratase / isomeraseAdd BLAST281
Regioni282 – 5713-hydroxyacyl-CoA dehydrogenaseAdd BLAST290

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi720 – 722Microbody targeting signal3

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.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiP07896.
KOiK07514.
OMAiYRMPGGT.
OrthoDBiEOG091G082G.
PhylomeDBiP07896.
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. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI
60 70 80 90 100
CGANGNFCAG ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG
110 120 130 140 150
GLELALGCHY RIANAKARVG LPEVTLGILP GARGTQLLPR VVGVPVALDL
160 170 180 190 200
ITSGKYLSAD EALRLGILDA VVKSDPVEEA IKFAQKIIDK PIEPRRIFNK
210 220 230 240 250
PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV KHPYEVGIKE
260 270 280 290 300
EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG
310 320 330 340 350
VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA
360 370 380 390 400
HQNGQASAKP KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK
410 420 430 440 450
PGAFLCTNTS ALNVDDIASS TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS
460 470 480 490 500
SPTTIATVMS LSKKIGKIGV VVGNCYGFVG NRMLAPYYNQ GFFLLEEGSK
510 520 530 540 550
PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG PSLPPGTPVR
560 570 580 590 600
KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS
610 620 630 640 650
QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL
660 670 680 690 700
HGYGWPRHKG GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL
710 720
VAQGSPPLKE WQSLAGPHGS KL
Length:722
Mass (Da):78,658
Last modified:January 23, 2007 - v2
Checksum:i76ACC709C5F23E86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03249 mRNA. Translation: AAA41825.1.
BC089777 mRNA. Translation: AAH89777.1.
J02748 Genomic DNA. Translation: AAA41826.1.
PIRiA23575. DWRTEP.
RefSeqiNP_598290.1. NM_133606.1.
UniGeneiRn.3671.

Genome annotation databases

EnsembliENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770.
GeneIDi171142.
KEGGirno:171142.
UCSCiRGD:621441. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03249 mRNA. Translation: AAA41825.1.
BC089777 mRNA. Translation: AAH89777.1.
J02748 Genomic DNA. Translation: AAA41826.1.
PIRiA23575. DWRTEP.
RefSeqiNP_598290.1. NM_133606.1.
UniGeneiRn.3671.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZCJX-ray1.90A260-722[»]
2X58X-ray2.80A/B1-722[»]
3ZW8X-ray2.50A/B1-722[»]
3ZW9X-ray2.90A/B1-722[»]
3ZWAX-ray2.47A/B1-722[»]
3ZWBX-ray3.10A/B1-722[»]
3ZWCX-ray2.30A/B1-722[»]
5AAJX-ray2.49A/B1-722[»]
5AAKX-ray2.80A/B1-722[»]
ProteinModelPortaliP07896.
SMRiP07896.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07896. 6 interactors.
STRINGi10116.ENSRNOP00000002410.

Chemistry databases

ChEMBLiCHEMBL3232.
SwissLipidsiSLP:000001144.

PTM databases

iPTMnetiP07896.
PhosphoSitePlusiP07896.

Proteomic databases

PaxDbiP07896.
PRIDEiP07896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770.
GeneIDi171142.
KEGGirno:171142.
UCSCiRGD:621441. rat.

Organism-specific databases

CTDi1962.
RGDi621441. Ehhadh.

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1250. LUCA.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiP07896.
KOiK07514.
OMAiYRMPGGT.
OrthoDBiEOG091G082G.
PhylomeDBiP07896.
TreeFamiTF316708.

Enzyme and pathway databases

UniPathwayiUPA00659.
BRENDAi4.2.1.17. 5301.
ReactomeiR-RNO-390918. Peroxisomal lipid metabolism.
SABIO-RKP07896.

Miscellaneous databases

EvolutionaryTraceiP07896.
PROiP07896.

Gene expression databases

BgeeiENSRNOG00000001770.
GenevisibleiP07896. RN.

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. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiECHP_RAT
AccessioniPrimary (citable) accession number: P07896
Secondary accession number(s): Q5EBD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.