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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

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 sitei101 – 1011Substrate; via amide nitrogenBy similarity
Sitei104 – 1041Important for catalytic activityBy similarity
Sitei124 – 1241Important 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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723Peroxisomal bifunctional enzymePRO_0000353181Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysineBy similarity
Modified residuei165 – 1651N6-acetyllysine; alternateBy similarity
Modified residuei165 – 1651N6-succinyllysine; alternateBy similarity
Modified residuei171 – 1711N6-acetyllysineBy similarity
Modified residuei219 – 2191N6-acetyllysine; alternateBy similarity
Modified residuei219 – 2191N6-succinyllysine; alternateBy similarity
Modified residuei250 – 2501N6-acetyllysineBy similarity
Modified residuei280 – 2801N6-succinyllysineBy similarity
Modified residuei290 – 2901N6-succinyllysineBy similarity
Modified residuei346 – 3461N6-acetyllysineBy similarity
Modified residuei350 – 3501N6-acetyllysineBy similarity
Modified residuei464 – 4641N6-acetyllysineBy similarity
Modified residuei532 – 5321N6-succinyllysineBy similarity
Modified residuei548 – 5481PhosphothreonineBy similarity
Modified residuei577 – 5771N6-succinyllysineBy similarity
Modified residuei584 – 5841N6-acetyllysine; alternateBy similarity
Modified residuei584 – 5841N6-succinyllysine; alternateBy similarity
Modified residuei591 – 5911N6-acetyllysine; alternateBy similarity
Modified residuei591 – 5911N6-succinyllysine; alternateBy similarity
Modified residuei710 – 7101N6-acetyllysine; alternateBy similarity
Modified residuei710 – 7101N6-succinyllysine; alternateBy similarity
Modified residuei722 – 7221N6-succinyllysineBy similarity

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.
SMRiQ5R5M8. Positions 262-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 282282Enoyl-CoA hydratase / isomeraseAdd
BLAST
Regioni283 – 5722903-hydroxyacyl-CoA dehydrogenaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi721 – 7233Microbody 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

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 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.

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.
SMRiQ5R5M8. Positions 262-717.
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

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 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 German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

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: June 24, 2015
This is version 79 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.