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P55100

- ECHP_CAVPO

UniProt

P55100 - ECHP_CAVPO

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Protein
Peroxisomal bifunctional enzyme
Gene
EHHADH
Organism
Cavia porcellus (Guinea pig)
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 sitei103 – 1031Substrate; via amide nitrogen By similarity
Sitei106 – 1061Important for catalytic activity By similarity
Sitei126 – 1261Important 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
Complete GO annotation...

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447: Unplaced

Subcellular locationi

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 – 726726Peroxisomal bifunctional enzyme
PRO_0000109246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysine By similarity
Modified residuei167 – 1671N6-acetyllysine; alternate By similarity
Modified residuei167 – 1671N6-succinyllysine; alternate By similarity
Modified residuei173 – 1731N6-acetyllysine By similarity
Modified residuei185 – 1851N6-succinyllysine By similarity
Modified residuei221 – 2211N6-acetyllysine; alternate By similarity
Modified residuei221 – 2211N6-succinyllysine; alternate By similarity
Modified residuei282 – 2821N6-succinyllysine By similarity
Modified residuei292 – 2921N6-succinyllysine By similarity
Modified residuei333 – 3331N6-succinyllysine By similarity
Modified residuei348 – 3481N6-acetyllysine By similarity
Modified residuei352 – 3521N6-acetyllysine By similarity
Modified residuei467 – 4671N6-acetyllysine By similarity
Modified residuei535 – 5351N6-succinyllysine By similarity
Modified residuei587 – 5871N6-acetyllysine; alternate By similarity
Modified residuei587 – 5871N6-succinyllysine; alternate By similarity
Modified residuei594 – 5941N6-acetyllysine; alternate By similarity
Modified residuei594 – 5941N6-succinyllysine; alternate By similarity
Modified residuei713 – 7131N6-acetyllysine; alternate By similarity
Modified residuei713 – 7131N6-succinyllysine; alternate By similarity
Modified residuei725 – 7251N6-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-348. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids 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. Positions 264-720.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 284284Enoyl-CoA hydratase / isomerase
Add
BLAST
Regioni285 – 5752913-hydroxyacyl-CoA dehydrogenase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi724 – 7263Microbody 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

eggNOGiCOG1250.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiP55100.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006176. 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.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55100-1 [UniParc]FASTAAdd to Basket

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MAEYLRLPHS LALIRLRNPP VNAISPAVIH GIKEGLQKAM SDYTIKGIVI    50
SGANNIFCAG ADIHGFSAPL SFGTGSGLGP IVDEMQRYEK PVVAAIQGMA 100
LGGGLELSLG CHYRIAHAEA RIGFPEVTLG ILPGARGTQL LPRLIGVPAA 150
LDLITSGRHI TAGEALKLGI LDKVVNSAPV EEAIKFAQKI LNQPLEPRRI 200
LNRPVSSLPN MDAIFGEAVE KMRRQHPGQL APETCVRSVQ ASVQYPYEGG 250
IMKERELFLN LQHSGQAKAL QYAFFAERSA PKWSTPSGAS WKTAAARPVS 300
SVGVLGLGTM GRGIAISFAR VGIPVIAVES DPKQLETAQK LITSILEKEA 350
SKSRQQCGQQ RSGPKPRFSS SMKDLASVDL VVEAVFEDMN LKKRVFAELS 400
AVCKPEAFLC TNTSALDVDE IATSTNRPQQ VIGTHFFSPA HVMKLLEVIP 450
SRHSSPTTIA TVMDLAKKIK KVAVVVGNCY GFVGNRMLRS YYEQTNFLLE 500
DGSKPEDIDQ ALEEFGFRMG PFRVSDLAGL DVGWKIRKGQ GLTGPSLQGT 550
APARKRGNAR YSPIADMLCE LGRFGQKTGQ GWYKYDKPLG RIHKPDPWLS 600
KFLSEYRETH HIKPRVIGRD EILERCLYAL INEAFRILGE GIAASPEHID 650
VIYLHGYGWP RHKGGPMFYA ASVGLPTVLE KLQKYYQQNP DIPHLEPCNY 700
LKKLASQGNP PLKEWQSLAG LPSSKL 726
Length:726
Mass (Da):79,375
Last modified:January 23, 2007 - v2
Checksum:iF1702122D62C5FF3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92742 mRNA. Translation: CAA63403.1.
X85112 mRNA. Translation: CAA59431.1.
PIRiS68697. S57651.
RefSeqiNP_001166417.1. NM_001172946.1.

Genome annotation databases

GeneIDi100135519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92742 mRNA. Translation: CAA63403.1 .
X85112 mRNA. Translation: CAA59431.1 .
PIRi S68697. S57651.
RefSeqi NP_001166417.1. NM_001172946.1.

3D structure databases

ProteinModelPortali P55100.
SMRi P55100. Positions 264-720.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10141.ENSCPOP00000019312.

Proteomic databases

PRIDEi P55100.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100135519.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261347.
HOVERGENi HBG104990.
InParanoidi P55100.

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 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 PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver."
    Caira F., Cherkaoui-Malki M., Hoefler G., Latruffe N.
    FEBS Lett. 378:57-60(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiECHP_CAVPO
AccessioniPrimary (citable) accession number: P55100
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 105 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

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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