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Q5R5M8

- ECHP_PONAB

UniProt

Q5R5M8 - ECHP_PONAB

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Protein
Peroxisomal bifunctional enzyme
Gene
EHHADH, ECHD
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011Substrate; via amide nitrogen By similarity
Sitei104 – 1041Important for catalytic activity By similarity
Sitei124 – 1241Important for catalytic activity By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
  2. coenzyme binding Source: InterPro
  3. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
  4. enoyl-CoA hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
  2. internal protein amino acid acetylation Source: UniProtKB
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: Unplaced

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723Peroxisomal bifunctional enzyme
PRO_0000353181Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiQ5R5M8.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5R5M8.
SMRiQ5R5M8. Positions 262-717.

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi721 – 7233Microbody targeting signal By similarity

Sequence similaritiesi

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

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.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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

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MAEYTRLHNA LALIRLRNPP VNAISTALLR DIKEGLQKAV IDHTIKAIVI    50
CGAEGKFSAG ADIHGFSAPR TFGFTLGHVV DEIQRNEKPV VAAIQGMAFG 100
GGLELALGCH YRIAHSEAQV GLPEVTLGLL PGARGTQLLP RLIGVPAALD 150
LITSGRHILA DEALKLGILD KVVNSDPVEE AIRFAQRVSD QPLESRRLCN 200
KPIQSLPNMD TIFSEALLKM RRQHPGCLAQ EACVRAVQAA VQYPYEVGVK 250
KEEELFLYLF QSGQARALQY AFLAERKANK WSTPSGASWK TASARPVSSV 300
GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK 350
MQQSGHPWSG PKPRLTSSMK ELGGVDLVIE AVFEEMSLKK QVFAELSAIC 400
KPEAFLCTNT SALDVDEIAS STDRPHLVIG THFFSPAHVM KLLEVIPSQY 450
SSPTTIATVM NLSKKIKKIG VVVGNCFGFV GNRMLNPYYN QAYFLLEEGS 500
KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT GPTLPPGTPA 550
RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KADPWLSKFL 600
SQYRETHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY 650
LHGYGWPRHK GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK 700
LASQGNPPQK EWQSLAGSPS SKL 723
Length:723
Mass (Da):79,481
Last modified:December 21, 2004 - v1
Checksum:i8CAE3A1578A147C6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CR860829 mRNA. Translation: CAH92938.1 .
RefSeqi NP_001127606.1. NM_001134134.1.

3D structure databases

ProteinModelPortali Q5R5M8.
SMRi Q5R5M8. Positions 262-717.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R5M8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100174685.
KEGGi pon:100174685.

Organism-specific databases

CTDi 1962.

Phylogenomic databases

HOGENOMi HOG000261347.
HOVERGENi HBG104990.
InParanoidi Q5R5M8.
KOi K07514.

Enzyme and pathway databases

UniPathwayi UPA00659 .

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR018376. Enoyl-CoA_hyd/isom_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 11, 2014
This is version 73 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

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