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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 nitrogenBy similarity
Sitei106 – 1061Important for catalytic activityBy similarity
Sitei126 – 1261Important for catalytic activityBy 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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447: Unplaced

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 726726Peroxisomal bifunctional enzymePRO_0000109246Add
BLAST

Amino acid modifications

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

Family & Domainsi

Region

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

Motif

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

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

« Hide

        10         20         30         40         50
MAEYLRLPHS LALIRLRNPP VNAISPAVIH GIKEGLQKAM SDYTIKGIVI
60 70 80 90 100
SGANNIFCAG ADIHGFSAPL SFGTGSGLGP IVDEMQRYEK PVVAAIQGMA
110 120 130 140 150
LGGGLELSLG CHYRIAHAEA RIGFPEVTLG ILPGARGTQL LPRLIGVPAA
160 170 180 190 200
LDLITSGRHI TAGEALKLGI LDKVVNSAPV EEAIKFAQKI LNQPLEPRRI
210 220 230 240 250
LNRPVSSLPN MDAIFGEAVE KMRRQHPGQL APETCVRSVQ ASVQYPYEGG
260 270 280 290 300
IMKERELFLN LQHSGQAKAL QYAFFAERSA PKWSTPSGAS WKTAAARPVS
310 320 330 340 350
SVGVLGLGTM GRGIAISFAR VGIPVIAVES DPKQLETAQK LITSILEKEA
360 370 380 390 400
SKSRQQCGQQ RSGPKPRFSS SMKDLASVDL VVEAVFEDMN LKKRVFAELS
410 420 430 440 450
AVCKPEAFLC TNTSALDVDE IATSTNRPQQ VIGTHFFSPA HVMKLLEVIP
460 470 480 490 500
SRHSSPTTIA TVMDLAKKIK KVAVVVGNCY GFVGNRMLRS YYEQTNFLLE
510 520 530 540 550
DGSKPEDIDQ ALEEFGFRMG PFRVSDLAGL DVGWKIRKGQ GLTGPSLQGT
560 570 580 590 600
APARKRGNAR YSPIADMLCE LGRFGQKTGQ GWYKYDKPLG RIHKPDPWLS
610 620 630 640 650
KFLSEYRETH HIKPRVIGRD EILERCLYAL INEAFRILGE GIAASPEHID
660 670 680 690 700
VIYLHGYGWP RHKGGPMFYA ASVGLPTVLE KLQKYYQQNP DIPHLEPCNY
710 720
LKKLASQGNP PLKEWQSLAG LPSSKL
Length:726
Mass (Da):79,375
Last modified:January 23, 2007 - v2
Checksum:iF1702122D62C5FF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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: October 29, 2014
This is version 107 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