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Protein

Peroxisomal bifunctional enzyme

Gene

EHHADH

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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.

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 sitei101Substrate; via amide nitrogenBy similarity1
Sitei104Important for catalytic activityBy similarity1
Sitei124Important for catalytic activityBy similarity1

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003531811 – 723Peroxisomal bifunctional enzymeAdd BLAST723

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei165N6-acetyllysine; alternateBy similarity1
Modified residuei165N6-succinyllysine; alternateBy similarity1
Modified residuei171N6-acetyllysineBy similarity1
Modified residuei219N6-acetyllysine; alternateBy similarity1
Modified residuei219N6-succinyllysine; alternateBy similarity1
Modified residuei250N6-acetyllysineBy similarity1
Modified residuei280N6-succinyllysineBy similarity1
Modified residuei290N6-succinyllysineBy similarity1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei350N6-acetyllysineBy similarity1
Modified residuei464N6-acetyllysineBy similarity1
Modified residuei532N6-succinyllysineBy similarity1
Modified residuei548PhosphothreonineBy similarity1
Modified residuei577N6-succinyllysineBy similarity1
Modified residuei584N6-acetyllysine; alternateBy similarity1
Modified residuei584N6-succinyllysine; alternateBy similarity1
Modified residuei591N6-acetyllysine; alternateBy similarity1
Modified residuei591N6-succinyllysine; alternateBy similarity1
Modified residuei710N6-acetyllysine; alternateBy similarity1
Modified residuei710N6-succinyllysine; alternateBy similarity1
Modified residuei718PhosphoserineBy similarity1
Modified residuei722N6-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-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ5R5M8.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000016064.

Structurei

3D structure databases

ProteinModelPortaliQ5R5M8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 282Enoyl-CoA hydratase / isomeraseAdd BLAST282
Regioni283 – 5723-hydroxyacyl-CoA dehydrogenaseAdd BLAST290

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi721 – 723Microbody 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.
InParanoidiQ5R5M8.
KOiK07514.

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.

Q5R5M8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYTRLHNA LALIRLRNPP VNAISTALLR DIKEGLQKAV IDHTIKAIVI
60 70 80 90 100
CGAEGKFSAG ADIHGFSAPR TFGFTLGHVV DEIQRNEKPV VAAIQGMAFG
110 120 130 140 150
GGLELALGCH YRIAHSEAQV GLPEVTLGLL PGARGTQLLP RLIGVPAALD
160 170 180 190 200
LITSGRHILA DEALKLGILD KVVNSDPVEE AIRFAQRVSD QPLESRRLCN
210 220 230 240 250
KPIQSLPNMD TIFSEALLKM RRQHPGCLAQ EACVRAVQAA VQYPYEVGVK
260 270 280 290 300
KEEELFLYLF QSGQARALQY AFLAERKANK WSTPSGASWK TASARPVSSV
310 320 330 340 350
GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK
360 370 380 390 400
MQQSGHPWSG PKPRLTSSMK ELGGVDLVIE AVFEEMSLKK QVFAELSAIC
410 420 430 440 450
KPEAFLCTNT SALDVDEIAS STDRPHLVIG THFFSPAHVM KLLEVIPSQY
460 470 480 490 500
SSPTTIATVM NLSKKIKKIG VVVGNCFGFV GNRMLNPYYN QAYFLLEEGS
510 520 530 540 550
KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT GPTLPPGTPA
560 570 580 590 600
RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KADPWLSKFL
610 620 630 640 650
SQYRETHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY
660 670 680 690 700
LHGYGWPRHK GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK
710 720
LASQGNPPQK EWQSLAGSPS SKL
Length:723
Mass (Da):79,481
Last modified:December 21, 2004 - v1
Checksum:i8CAE3A1578A147C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860829 mRNA. Translation: CAH92938.1.
RefSeqiNP_001127606.1. NM_001134134.1.

Genome annotation databases

GeneIDi100174685.
KEGGipon:100174685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860829 mRNA. Translation: CAH92938.1.
RefSeqiNP_001127606.1. NM_001134134.1.

3D structure databases

ProteinModelPortaliQ5R5M8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000016064.

Proteomic databases

PRIDEiQ5R5M8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100174685.
KEGGipon:100174685.

Organism-specific databases

CTDi1962.

Phylogenomic databases

eggNOGiKOG1683. Eukaryota.
COG1250. LUCA.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiQ5R5M8.
KOiK07514.

Enzyme and pathway databases

UniPathwayiUPA00659.

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_PONAB
AccessioniPrimary (citable) accession number: Q5R5M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: December 21, 2004
Last modified: October 5, 2016
This is version 85 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

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.