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P07896

- ECHP_RAT

UniProt

P07896 - ECHP_RAT

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Protein

Peroxisomal bifunctional enzyme

Gene

Ehhadh

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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 sitei100 – 1001Substrate; via amide nitrogenBy similarity
Sitei103 – 1031Important for catalytic activityBy similarity
Sitei123 – 1231Important for catalytic activityBy similarity

GO - Molecular functioni

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

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

SABIO-RKP07896.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 11

Organism-specific databases

RGDi621441. Ehhadh.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: Ensembl
  3. nucleus Source: Ensembl
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Peroxisomal bifunctional enzymePRO_0000109249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ala)
Modified residuei38 – 381N6-succinyllysineBy similarity
Modified residuei173 – 1731N6-acetyllysine; alternateBy similarity
Modified residuei173 – 1731N6-succinyllysine; alternateBy similarity
Modified residuei182 – 1821N6-succinyllysineBy similarity
Modified residuei190 – 1901N6-acetyllysine; alternateBy similarity
Modified residuei190 – 1901N6-succinyllysine; alternateBy similarity
Modified residuei218 – 2181N6-acetyllysine; alternateBy similarity
Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity
Modified residuei241 – 2411N6-succinyllysineBy similarity
Modified residuei249 – 2491N6-acetyllysineBy similarity
Modified residuei253 – 2531N6-succinyllysineBy similarity
Modified residuei275 – 2751N6-acetyllysine; alternateBy similarity
Modified residuei275 – 2751N6-succinyllysine; alternateBy similarity
Modified residuei279 – 2791N6-succinyllysineBy similarity
Modified residuei289 – 2891N6-succinyllysineBy similarity
Modified residuei330 – 3301N6-succinyllysineBy similarity
Modified residuei345 – 3451N6-acetyllysineBy similarity
Modified residuei359 – 3591N6-acetyllysineBy similarity
Modified residuei463 – 4631N6-acetyllysineBy similarity
Modified residuei531 – 5311N6-succinyllysineBy similarity
Modified residuei576 – 5761N6-succinyllysineBy similarity
Modified residuei583 – 5831N6-acetyllysine; alternateBy similarity
Modified residuei583 – 5831N6-succinyllysine; alternateBy similarity
Modified residuei590 – 5901N6-acetyllysine; alternateBy similarity
Modified residuei590 – 5901N6-succinyllysine; alternateBy similarity
Modified residuei709 – 7091N6-acetyllysine; alternateBy similarity
Modified residuei709 – 7091N6-succinyllysine; alternateBy similarity
Modified residuei721 – 7211N6-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-345. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP07896.
PRIDEiP07896.

PTM databases

PhosphoSiteiP07896.

Expressioni

Gene expression databases

GenevestigatoriP07896.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiP07896. 6 interactions.
STRINGi10116.ENSRNOP00000002410.

Structurei

Secondary structure

1
722
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Turni8 – 103
Beta strandi11 – 166
Turni19 – 224
Helixi26 – 4015
Beta strandi47 – 537
Beta strandi63 – 653
Beta strandi67 – 693
Helixi74 – 8411
Beta strandi89 – 935
Beta strandi95 – 984
Helixi100 – 1067
Beta strandi108 – 1147
Beta strandi118 – 1203
Helixi122 – 1265
Turni131 – 1333
Helixi134 – 1429
Helixi144 – 15310
Beta strandi156 – 1583
Helixi159 – 1646
Beta strandi169 – 1746
Helixi176 – 18712
Beta strandi188 – 1903
Helixi193 – 1953
Helixi197 – 1993
Helixi208 – 22215
Helixi227 – 24115
Helixi244 – 25916
Helixi262 – 27211
Helixi273 – 2786
Turni283 – 2853
Turni288 – 2903
Beta strandi298 – 3025
Helixi306 – 31611
Turni317 – 3193
Beta strandi321 – 3255
Helixi329 – 35224
Beta strandi353 – 3553
Beta strandi362 – 3665
Helixi368 – 3714
Beta strandi375 – 3795
Helixi385 – 39814
Beta strandi404 – 4074
Beta strandi410 – 4123
Helixi414 – 4185
Helixi424 – 4263
Beta strandi427 – 4326
Turni436 – 4383
Beta strandi441 – 4466
Helixi452 – 46413
Beta strandi468 – 4725
Turni476 – 4794
Helixi480 – 49617
Helixi501 – 51111
Helixi517 – 5248
Helixi526 – 53510
Beta strandi538 – 5414
Helixi560 – 5667
Turni572 – 5754
Beta strandi576 – 5838
Beta strandi589 – 5913
Helixi593 – 60513
Helixi615 – 63521
Beta strandi638 – 6403
Helixi642 – 65211
Helixi657 – 6593
Helixi662 – 6698
Helixi671 – 68414
Helixi689 – 6913
Helixi695 – 7028
Helixi708 – 7103
Helixi711 – 7155

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCJX-ray1.90A260-722[»]
2X58X-ray2.80A/B1-722[»]
3ZW8X-ray2.50A/B1-722[»]
3ZW9X-ray2.90A/B1-722[»]
3ZWAX-ray2.47A/B1-722[»]
3ZWBX-ray3.10A/B1-722[»]
3ZWCX-ray2.30A/B1-722[»]
ProteinModelPortaliP07896.
SMRiP07896. Positions 261-719.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07896.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 281281Enoyl-CoA hydratase / isomeraseAdd
BLAST
Regioni282 – 5712903-hydroxyacyl-CoA dehydrogenaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi720 – 7223Microbody targeting signal

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.
GeneTreeiENSGT00720000108673.
HOGENOMiHOG000261347.
HOVERGENiHBG104990.
InParanoidiP07896.
KOiK07514.
OMAiLKMRKQH.
OrthoDBiEOG725DH0.
PhylomeDBiP07896.
TreeFamiTF316708.

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.

P07896 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI
60 70 80 90 100
CGANGNFCAG ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG
110 120 130 140 150
GLELALGCHY RIANAKARVG LPEVTLGILP GARGTQLLPR VVGVPVALDL
160 170 180 190 200
ITSGKYLSAD EALRLGILDA VVKSDPVEEA IKFAQKIIDK PIEPRRIFNK
210 220 230 240 250
PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV KHPYEVGIKE
260 270 280 290 300
EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG
310 320 330 340 350
VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA
360 370 380 390 400
HQNGQASAKP KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK
410 420 430 440 450
PGAFLCTNTS ALNVDDIASS TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS
460 470 480 490 500
SPTTIATVMS LSKKIGKIGV VVGNCYGFVG NRMLAPYYNQ GFFLLEEGSK
510 520 530 540 550
PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG PSLPPGTPVR
560 570 580 590 600
KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS
610 620 630 640 650
QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL
660 670 680 690 700
HGYGWPRHKG GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL
710 720
VAQGSPPLKE WQSLAGPHGS KL
Length:722
Mass (Da):78,658
Last modified:January 23, 2007 - v2
Checksum:i76ACC709C5F23E86
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K03249 mRNA. Translation: AAA41825.1.
BC089777 mRNA. Translation: AAH89777.1.
J02748 Genomic DNA. Translation: AAA41826.1.
PIRiA23575. DWRTEP.
RefSeqiNP_598290.1. NM_133606.1.
UniGeneiRn.3671.

Genome annotation databases

EnsembliENSRNOT00000002410; ENSRNOP00000002410; ENSRNOG00000001770.
GeneIDi171142.
KEGGirno:171142.
UCSCiRGD:621441. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
K03249 mRNA. Translation: AAA41825.1 .
BC089777 mRNA. Translation: AAH89777.1 .
J02748 Genomic DNA. Translation: AAA41826.1 .
PIRi A23575. DWRTEP.
RefSeqi NP_598290.1. NM_133606.1.
UniGenei Rn.3671.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZCJ X-ray 1.90 A 260-722 [» ]
2X58 X-ray 2.80 A/B 1-722 [» ]
3ZW8 X-ray 2.50 A/B 1-722 [» ]
3ZW9 X-ray 2.90 A/B 1-722 [» ]
3ZWA X-ray 2.47 A/B 1-722 [» ]
3ZWB X-ray 3.10 A/B 1-722 [» ]
3ZWC X-ray 2.30 A/B 1-722 [» ]
ProteinModelPortali P07896.
SMRi P07896. Positions 261-719.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P07896. 6 interactions.
STRINGi 10116.ENSRNOP00000002410.

Chemistry

ChEMBLi CHEMBL3232.

PTM databases

PhosphoSitei P07896.

Proteomic databases

PaxDbi P07896.
PRIDEi P07896.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000002410 ; ENSRNOP00000002410 ; ENSRNOG00000001770 .
GeneIDi 171142.
KEGGi rno:171142.
UCSCi RGD:621441. rat.

Organism-specific databases

CTDi 1962.
RGDi 621441. Ehhadh.

Phylogenomic databases

eggNOGi COG1250.
GeneTreei ENSGT00720000108673.
HOGENOMi HOG000261347.
HOVERGENi HBG104990.
InParanoidi P07896.
KOi K07514.
OMAi LKMRKQH.
OrthoDBi EOG725DH0.
PhylomeDBi P07896.
TreeFami TF316708.

Enzyme and pathway databases

UniPathwayi UPA00659 .
SABIO-RK P07896.

Miscellaneous databases

EvolutionaryTracei P07896.
NextBioi 621936.
PROi P07896.

Gene expression databases

Genevestigatori P07896.

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

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."
    Osumi T., Ishii N., Hijikata M., Kamijo K., Ozasa H., Furuta S., Miyazawa S., Kondo K., Inoue K., Kagamiyama H., Hashimoto T.
    J. Biol. Chem. 260:8905-8910(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  3. "Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme."
    Ishii N., Hijikata M., Osumi T., Hashimoto T.
    J. Biol. Chem. 262:8144-8150(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
  4. "Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins."
    Dieuaide-Noubhani M., Novikov D., Baumgart E., Vanhooren J.C.T., Fransen M., Goethals M., Vandekerckhove J., Van Veldhoven P.P., Mannaerts G.P.
    Eur. J. Biochem. 240:660-666(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 260-265; 294-302; 520-531 AND 710-719.
  5. "Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities."
    Palosaari P.M., Hiltunen J.K.
    J. Biol. Chem. 265:2446-2449(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ISOMERASE.
  6. "Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1."
    Taskinen J.P., Kiema T.R., Hiltunen J.K., Wierenga R.K.
    J. Mol. Biol. 355:734-746(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 260-722, SUBUNIT.

Entry informationi

Entry nameiECHP_RAT
AccessioniPrimary (citable) accession number: P07896
Secondary accession number(s): Q5EBD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 138 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

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3