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P97852

- DHB4_RAT

UniProt

P97852 - DHB4_RAT

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Protein
Peroxisomal multifunctional enzyme type 2
Gene
Hsd17b4, Edh17b4
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Bifunctional enzyme acting on the peroxisomal beta-oxidation pathway for fatty acids. Catalyzes the formation of 3-ketoacyl-CoA intermediates from both straight-chain and 2-methyl-branched-chain fatty acids.

Catalytic activityi

(R)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.
(24R,25R)-3-alpha,7-alpha,12-alpha,24-tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H2O.
(3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211NAD; via amide nitrogen By similarity
Binding sitei40 – 401NAD By similarity
Binding sitei99 – 991NAD; via carbonyl oxygen By similarity
Binding sitei151 – 1511Substrate
Active sitei164 – 1641Proton acceptor
Binding sitei434 – 4341(3R)-3-hydroxydecanoyl-CoA By similarity
Binding sitei532 – 5321(3R)-3-hydroxydecanoyl-CoA; via amide nitrogen By similarity
Binding sitei562 – 5621(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygen By similarity
Binding sitei705 – 7051Substrate By similarity
Binding sitei723 – 7231Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 4025NAD
Add
BLAST
Nucleotide bindingi75 – 762NAD By similarity
Nucleotide bindingi164 – 1685NAD By similarity
Nucleotide bindingi196 – 1994NAD By similarity

GO - Molecular functioni

  1. 17-beta-hydroxysteroid dehydrogenase (NAD+) activity Source: Ensembl
  2. 3-hydroxyacyl-CoA dehydrogenase activity Source: Ensembl
  3. 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity Source: UniProtKB-EC
  4. isomerase activity Source: UniProtKB-KW
  5. long-chain-enoyl-CoA hydratase activity Source: Ensembl
  6. testosterone dehydrogenase [NAD(P)] activity Source: RGD
Complete GO annotation...

GO - Biological processi

  1. Sertoli cell development Source: Ensembl
  2. androgen metabolic process Source: Ensembl
  3. cholesterol metabolic process Source: RGD
  4. estrogen metabolic process Source: Ensembl
  5. fatty acid beta-oxidation Source: UniProtKB-UniPathway
  6. medium-chain fatty-acyl-CoA metabolic process Source: Ensembl
  7. very long-chain fatty acid metabolic process Source: Ensembl
  8. very long-chain fatty-acyl-CoA metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14329.
ReactomeiREACT_198818. alpha-linolenic acid (ALA) metabolism.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal multifunctional enzyme type 2
Short name:
MFE-2
Alternative name(s):
17-beta-hydroxysteroid dehydrogenase 4
Short name:
17-beta-HSD 4
D-bifunctional protein
Short name:
DBP
Multifunctional protein 2
Short name:
MPF-2
Cleaved into the following 2 chains:
Alternative name(s):
3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
Gene namesi
Name:Hsd17b4
Synonyms:Edh17b4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 18

Organism-specific databases

RGDi621806. Hsd17b4.

Subcellular locationi

Peroxisome 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
  2. peroxisomal membrane Source: Ensembl
  3. peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Peroxisomal multifunctional enzyme type 2
PRO_0000054585Add
BLAST
Chaini1 – 311311(3R)-hydroxyacyl-CoA dehydrogenase
PRO_0000400086Add
BLAST
Chaini312 – 735424Enoyl-CoA hydratase 2
PRO_0000400087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysine; alternate By similarity
Modified residuei46 – 461N6-succinyllysine; alternate By similarity
Modified residuei57 – 571N6-succinyllysine By similarity
Modified residuei68 – 681N6-succinyllysine By similarity
Modified residuei84 – 841N6-succinyllysine By similarity
Modified residuei275 – 2751N6-succinyllysine By similarity
Modified residuei304 – 3041Phosphoserine By similarity
Modified residuei308 – 3081Phosphoserine By similarity
Modified residuei355 – 3551N6-succinyllysine By similarity
Modified residuei423 – 4231N6-succinyllysine By similarity
Modified residuei564 – 5641N6-acetyllysine By similarity
Modified residuei578 – 5781N6-succinyllysine By similarity
Modified residuei662 – 6621N6-succinyllysine By similarity
Modified residuei668 – 6681N6-acetyllysine By similarity
Modified residuei724 – 7241N6-succinyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP97852.
PRIDEiP97852.

PTM databases

PhosphoSiteiP97852.

Expressioni

Gene expression databases

GenevestigatoriP97852.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP97852. 1 interaction.
STRINGi10116.ENSRNOP00000043755.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144
Turni15 – 184
Helixi20 – 3112
Beta strandi35 – 395
Helixi53 – 6412
Beta strandi68 – 725
Helixi76 – 783
Helixi79 – 8911
Beta strandi95 – 984
Helixi108 – 1103
Helixi113 – 14129
Beta strandi144 – 1496
Helixi152 – 1565
Helixi162 – 18120
Helixi183 – 1853
Beta strandi187 – 1959
Turni199 – 2013
Helixi202 – 2043
Helixi207 – 2126
Helixi215 – 2173
Helixi219 – 2257
Beta strandi236 – 2405
Beta strandi243 – 2519
Helixi266 – 2716
Helixi273 – 2764
Helixi288 – 30215

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZ6X-ray2.38A/B/C/D1-319[»]
ProteinModelPortaliP97852.
SMRiP97852. Positions 3-303, 322-604, 621-735.

Miscellaneous databases

EvolutionaryTraceiP97852.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 599117MaoC-like
Add
BLAST
Domaini623 – 735113SCP2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 305305(3R)-hydroxyacyl-CoA dehydrogenase
Add
BLAST
Regioni321 – 621301Enoyl-CoA hydratase 2
Add
BLAST
Regioni405 – 4062(3R)-3-hydroxydecanoyl-CoA binding By similarity
Regioni509 – 5146(3R)-3-hydroxydecanoyl-CoA binding By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi733 – 7353Microbody targeting signal Reviewed prediction

Sequence similaritiesi

Contains 1 MaoC-like domain.
Contains 1 SCP2 domain.

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
KOiK12405.
OMAiTETIMPP.
OrthoDBiEOG7RBZ7V.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97852-1 [UniParc]FASTAAdd to Basket

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MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK    50
GSSAADKVVE EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA 100
GILRDRSFSR ISDEDWDIIQ RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA 150
SASGIYGNFG QANYSAAKLG LLGLANTLVI EGRKNNIHCN TIAPNAGSRM 200
TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE 250
RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH 300
KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV 350
GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF 400
AKVLHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK 450
ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPSRPPDA VLRDTTSLNQ 500
AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA RHVLQQFADN 550
DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA 600
YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE 650
WHITKNGNVA AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG 700
KLNPQNAFFS GRLKARGNIM LSQKLQMILK DYAKL 735
Length:735
Mass (Da):79,428
Last modified:January 23, 2007 - v3
Checksum:iE14F15FFD35FC7D8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 22MA → M in CAA64427. 1 Publication
Sequence conflicti12 – 121V → G in CAA64427. 1 Publication
Sequence conflicti26 – 261A → G in CAA64427. 1 Publication
Sequence conflicti76 – 761V → G in AAB09724. 1 Publication
Sequence conflicti106 – 1061R → P in CAA64427. 1 Publication
Sequence conflicti157 – 1571G → S in AAB09724. 1 Publication
Sequence conflicti284 – 2841K → E in CAA64427. 1 Publication
Sequence conflicti368 – 3681A → P in CAA64427. 1 Publication
Sequence conflicti376 – 3761F → I in CAA64427. 1 Publication
Sequence conflicti386 – 3861M → T in AAB09724. 1 Publication
Sequence conflicti485 – 4851S → D in AAB09724. 1 Publication
Sequence conflicti498 – 4981L → V in CAA64427. 1 Publication
Sequence conflicti521 – 5211S → G in CAA64427. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S83279 mRNA. Translation: AAB49519.1.
U37486 mRNA. Translation: AAB09724.1.
X94978 mRNA. Translation: CAA64427.1.
RefSeqiNP_077368.2. NM_024392.2.
UniGeneiRn.2082.

Genome annotation databases

EnsembliENSRNOT00000021646; ENSRNOP00000021646; ENSRNOG00000015840.
GeneIDi79244.
KEGGirno:79244.
UCSCiRGD:621806. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S83279 mRNA. Translation: AAB49519.1 .
U37486 mRNA. Translation: AAB09724.1 .
X94978 mRNA. Translation: CAA64427.1 .
RefSeqi NP_077368.2. NM_024392.2.
UniGenei Rn.2082.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GZ6 X-ray 2.38 A/B/C/D 1-319 [» ]
ProteinModelPortali P97852.
SMRi P97852. Positions 3-303, 322-604, 621-735.
ModBasei Search...

Protein-protein interaction databases

IntActi P97852. 1 interaction.
STRINGi 10116.ENSRNOP00000043755.

Chemistry

ChEMBLi CHEMBL1075219.

PTM databases

PhosphoSitei P97852.

Proteomic databases

PaxDbi P97852.
PRIDEi P97852.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021646 ; ENSRNOP00000021646 ; ENSRNOG00000015840 .
GeneIDi 79244.
KEGGi rno:79244.
UCSCi RGD:621806. rat.

Organism-specific databases

CTDi 3295.
RGDi 621806. Hsd17b4.

Phylogenomic databases

eggNOGi COG1028.
GeneTreei ENSGT00530000062928.
HOGENOMi HOG000170895.
HOVERGENi HBG002174.
KOi K12405.
OMAi TETIMPP.
OrthoDBi EOG7RBZ7V.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci MetaCyc:MONOMER-14329.
Reactomei REACT_198818. alpha-linolenic acid (ALA) metabolism.

Miscellaneous databases

EvolutionaryTracei P97852.
NextBioi 614694.
PROi P97852.

Gene expression databases

Genevestigatori P97852.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
[Graphical view ]
Pfami PF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMi SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-30; 32-44; 110-115; 132-139 AND 270-274, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
    Tissue: Liver.
  2. "Rat 17 beta-hydroxysteroid dehydrogenase type IV is a novel peroxisome proliferator-inducible gene."
    Corton J.C., Bocos C., Moreno E.S., Merritt A., Marsman D.S., Sausen P.J., Cattley R.C., Gustafsson J.-A.
    Mol. Pharmacol. 50:1157-1166(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization."
    Qin Y.M., Poutanen M.H., Helander H.M., Kvist A.P., Siivari K.M., Schmitz W., Conzelmann E., Hellman U., Hiltunen J.K.
    Biochem. J. 321:21-28(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 318-330; 479-505; 542-554; 562-576 AND 583-587, ENZYME CATALYSIS.
  4. "Identification and characterization of the 2-enoyl-CoA hydratases involved in peroxisomal beta-oxidation in rat liver."
    Dieuaide-Noubhani M., Novikov D., Vandekerckhove J., Veldhoven P.P., Mannaerts G.P.
    Biochem. J. 321:253-259(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 312-324, PROTEOLYTIC CLEAVAGE.
  5. "Binary structure of the two-domain (3R)-hydroxyacyl-CoA dehydrogenase from rat peroxisomal multifunctional enzyme type 2 at 2.38 A resolution."
    Haapalainen A.M., Koski M.K., Qin Y.-M., Hiltunen J.K., Glumoff T.
    Structure 11:87-97(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-319 IN COMPLEX WITH NAD, HOMODIMERIZATION.

Entry informationi

Entry nameiDHB4_RAT
AccessioniPrimary (citable) accession number: P97852
Secondary accession number(s): P70523, P70540
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The protein is found both as a full length peptide and in a cleaved version.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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

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