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Protein

Peroxisomal multifunctional enzyme type 2

Gene

Hsd17b4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei21NAD; via amide nitrogenBy similarity1
Binding sitei40NADBy similarity1
Binding sitei99NAD; via carbonyl oxygenBy similarity1
Binding sitei151Substrate1
Active sitei164Proton acceptor1
Binding sitei434(3R)-3-hydroxydecanoyl-CoABy similarity1
Binding sitei532(3R)-3-hydroxydecanoyl-CoA; via amide nitrogenBy similarity1
Binding sitei562(3R)-3-hydroxydecanoyl-CoA; via carbonyl oxygenBy similarity1
Binding sitei705SubstrateBy similarity1
Binding sitei723SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi16 – 40NAD1 PublicationAdd BLAST25
Nucleotide bindingi75 – 76NADBy similarity2
Nucleotide bindingi164 – 168NADBy similarity5
Nucleotide bindingi196 – 199NADBy similarity4

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • cholesterol metabolic process Source: RGD
  • fatty acid beta-oxidation Source: UniProtKB-UniPathway
  • response to drug Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to steroid hormone Source: RGD
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.
ReactomeiR-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-RNO-2046106. alpha-linolenic acid (ALA) metabolism.
R-RNO-389887. Beta-oxidation of pristanoyl-CoA.
R-RNO-390247. Beta-oxidation of very long chain fatty acids.
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
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi621806. Hsd17b4.

Subcellular locationi

GO - Cellular componenti

  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075219.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000545851 – 735Peroxisomal multifunctional enzyme type 2Add BLAST735
ChainiPRO_00004000861 – 311(3R)-hydroxyacyl-CoA dehydrogenaseAdd BLAST311
ChainiPRO_0000400087312 – 735Enoyl-CoA hydratase 2Add BLAST424

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei46N6-acetyllysine; alternateBy similarity1
Modified residuei46N6-succinyllysine; alternateBy similarity1
Modified residuei52PhosphoserineBy similarity1
Modified residuei57N6-succinyllysineBy similarity1
Modified residuei68N6-succinyllysineBy similarity1
Modified residuei84N6-succinyllysineBy similarity1
Modified residuei265PhosphothreonineBy similarity1
Modified residuei275N6-succinyllysineBy similarity1
Modified residuei304PhosphoserineBy similarity1
Modified residuei308PhosphoserineBy similarity1
Modified residuei355N6-succinyllysineBy similarity1
Modified residuei423N6-succinyllysineBy similarity1
Modified residuei564N6-acetyllysineBy similarity1
Modified residuei578N6-succinyllysineBy similarity1
Modified residuei662N6-succinyllysineBy similarity1
Modified residuei668N6-acetyllysineBy similarity1
Modified residuei724N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP97852.
PRIDEiP97852.

PTM databases

iPTMnetiP97852.
PhosphoSitePlusiP97852.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015840.
ExpressionAtlasiP97852. baseline and differential.
GenevisibleiP97852. RN.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiP97852. 1 interactor.
STRINGi10116.ENSRNOP00000021646.

Structurei

Secondary structure

1735
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Turni15 – 18Combined sources4
Helixi20 – 31Combined sources12
Beta strandi35 – 39Combined sources5
Helixi53 – 64Combined sources12
Beta strandi68 – 72Combined sources5
Helixi76 – 78Combined sources3
Helixi79 – 89Combined sources11
Beta strandi95 – 98Combined sources4
Helixi108 – 110Combined sources3
Helixi113 – 141Combined sources29
Beta strandi144 – 149Combined sources6
Helixi152 – 156Combined sources5
Helixi162 – 181Combined sources20
Helixi183 – 185Combined sources3
Beta strandi187 – 195Combined sources9
Turni199 – 201Combined sources3
Helixi202 – 204Combined sources3
Helixi207 – 212Combined sources6
Helixi215 – 217Combined sources3
Helixi219 – 225Combined sources7
Beta strandi236 – 240Combined sources5
Beta strandi243 – 251Combined sources9
Helixi266 – 271Combined sources6
Helixi273 – 276Combined sources4
Helixi288 – 302Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GZ6X-ray2.38A/B/C/D1-319[»]
ProteinModelPortaliP97852.
SMRiP97852.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97852.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini483 – 599MaoC-likeAdd BLAST117
Domaini623 – 735SCP2Add BLAST113

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 305(3R)-hydroxyacyl-CoA dehydrogenaseAdd BLAST305
Regioni321 – 621Enoyl-CoA hydratase 2Add BLAST301
Regioni405 – 406(3R)-3-hydroxydecanoyl-CoA bindingBy similarity2
Regioni509 – 514(3R)-3-hydroxydecanoyl-CoA bindingBy similarity6

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi733 – 735Microbody targeting signalSequence analysis3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP97852.
KOiK12405.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF54637. 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

« Hide

        10         20         30         40         50
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK
60 70 80 90 100
GSSAADKVVE EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA
110 120 130 140 150
GILRDRSFSR ISDEDWDIIQ RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA
160 170 180 190 200
SASGIYGNFG QANYSAAKLG LLGLANTLVI EGRKNNIHCN TIAPNAGSRM
210 220 230 240 250
TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG AGWIGKLRWE
260 270 280 290 300
RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH
310 320 330 340 350
KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV
360 370 380 390 400
GASVKNPKDL KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF
410 420 430 440 450
AKVLHGEQYL ELYKPLPRSG ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK
460 470 480 490 500
ELICYNQFSV FVVGSGGFGG KRTSEKLKAA VAVPSRPPDA VLRDTTSLNQ
510 520 530 540 550
AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA RHVLQQFADN
560 570 580 590 600
DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA
610 620 630 640 650
YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE
660 670 680 690 700
WHITKNGNVA AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG
710 720 730
KLNPQNAFFS GRLKARGNIM LSQKLQMILK DYAKL
Length:735
Mass (Da):79,428
Last modified:January 23, 2007 - v3
Checksum:iE14F15FFD35FC7D8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 2MA → M in CAA64427 (PubMed:8856068).Curated2
Sequence conflicti12V → G in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti26A → G in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti76V → G in AAB09724 (PubMed:9003397).Curated1
Sequence conflicti106R → P in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti157G → S in AAB09724 (PubMed:9003397).Curated1
Sequence conflicti284K → E in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti368A → P in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti376F → I in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti386M → T in AAB09724 (PubMed:9003397).Curated1
Sequence conflicti485S → D in AAB09724 (PubMed:9003397).Curated1
Sequence conflicti498L → V in CAA64427 (PubMed:8856068).Curated1
Sequence conflicti521S → G in CAA64427 (PubMed:8856068).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GZ6X-ray2.38A/B/C/D1-319[»]
ProteinModelPortaliP97852.
SMRiP97852.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97852. 1 interactor.
STRINGi10116.ENSRNOP00000021646.

Chemistry databases

ChEMBLiCHEMBL1075219.

PTM databases

iPTMnetiP97852.
PhosphoSitePlusiP97852.

Proteomic databases

PaxDbiP97852.
PRIDEiP97852.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3295.
RGDi621806. Hsd17b4.

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000062928.
HOGENOMiHOG000170895.
HOVERGENiHBG002174.
InParanoidiP97852.
KOiK12405.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciMetaCyc:MONOMER-14329.
ReactomeiR-RNO-193368. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
R-RNO-2046106. alpha-linolenic acid (ALA) metabolism.
R-RNO-389887. Beta-oxidation of pristanoyl-CoA.
R-RNO-390247. Beta-oxidation of very long chain fatty acids.

Miscellaneous databases

EvolutionaryTraceiP97852.
PROiP97852.

Gene expression databases

BgeeiENSRNOG00000015840.
ExpressionAtlasiP97852. baseline and differential.
GenevisibleiP97852. RN.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.30.1050.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF54637. SSF54637. 2 hits.
SSF55718. SSF55718. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 142 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.