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Reviewed, UniProtKB/Swiss-Prot P97852 (DHB4_RAT)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Peroxisomal multifunctional enzyme type 2
      Short name=MFE-2
Alternative name(s):
    D-bifunctional protein
      Short name=DBP
    17-beta-hydroxysteroid dehydrogenase 4
      Short name=17-beta-HSD 4
Including the following 2 domains:
    1- Recommended name:
            3-hydroxyacyl-CoA dehydrogenase
              EC=1.1.1.35
    2- Recommended name:
            3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase
              EC=4.2.1.107
Gene names
Name: Hsd17b4
Synonyms: Edh17b4
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length735 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 By similarity.

Catalytic activity

(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.

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Homodimer. Ref.2

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Contains 1 SCP2 domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 735734Peroxisomal multifunctional enzyme type 2
PRO_0000054585

Regions

Domain623 – 735113SCP2
Nucleotide binding16 – 4025NAD
Nucleotide binding75 – 762NAD By similarity
Nucleotide binding164 – 1685NAD By similarity
Nucleotide binding196 – 1994NAD By similarity
Region2 – 3053043-hydroxyacyl-CoA dehydrogenase
Region321 – 6213013-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase

Sites

Active site1641Proton acceptor
Binding site211NAD; via amide nitrogen By similarity
Binding site401NAD By similarity
Binding site991NAD; via carbonyl oxygen By similarity
Binding site1511Substrate
Binding site7051Substrate By similarity
Binding site7231Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31Phosphoserine By similarity
Modified residue2651Phosphothreonine By similarity
Modified residue3081Phosphoserine By similarity
Modified residue6621N6-acetyllysine By similarity

Secondary structure

1 .................................................. 735
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P97852-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E14F15FFD35FC7D8

FASTA73579,428
        10         20         30         40         50         60 
MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSSAADKVVE 

        70         80         90        100        110        120 
EIRRRGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIQ 

       130        140        150        160        170        180 
RVHLRGSFQV TRAAWDHMKK QNYGRIIMTA SASGIYGNFG QANYSAAKLG LLGLANTLVI 

       190        200        210        220        230        240 
EGRKNNIHCN TIAPNAGSRM TETVMPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG 

       250        260        270        280        290        300 
AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWVKICDFS NASKPKSIQE STGGIIEVLH 

       310        320        330        340        350        360 
KIDSEGISQN HTGQVASADA SGFAGVVGHK LPSFSSSYTE LQCIMYALGV GASVKNPKDL 

       370        380        390        400        410        420 
KFVYEGSADF SCLPTFGVIV AQKSLMSGGL AEVPGLSINF AKVLHGEQYL ELYKPLPRSG 

       430        440        450        460        470        480 
ELKCEAVIAD ILDKGSGIVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA 

       490        500        510        520        530        540 
VAVPSRPPDA VLRDTTSLNQ AALYRLSGDS NPLHIDPSFA SIAGFEKPIL HGLCTFGFSA 

       550        560        570        580        590        600 
RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVQ ETGDIVISNA 

       610        620        630        640        650        660 
YVDLVPTSGV SAQTPSEGGA LQSALVFGEI GRRLKDVGRE VVKKVNAVFE WHITKNGNVA 

       670        680        690        700        710        720 
AKWTIDLKNG SGEVYQGPAK GSADTTITIS DEDFMEVVLG KLNPQNAFFS GRLKARGNIM 

       730 
LSQKLQMILK DYAKL

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References

[1]"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: 8913347] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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: 12517343] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-319 IN COMPLEX WITH NAD, HOMODIMERIZATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

S83279 mRNA. Translation: AAB49519.1.
IPIIPI00561647.
RefSeqNP_077368.2.
UniGeneRn.2082

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GZ6X-ray2.38A/B/C/D1-319[»]
SMRP97852. Positions 321-603, 322-604, 620-734, 621-735.
ModBaseSearch...

Proteomic databases

PRIDEP97852.

Genome annotation databases

EnsemblENSRNOG00000015840. Rattus norvegicus. [Contig view]
GeneID79244.
KEGGrno:79244.

Organism-specific databases

RGD621806. Hsd17b4.

Phylogenomic databases

HOVERGENP97852.

Enzyme and pathway databases

BRENDA1.1.1.35. 248.
4.2.1.107. 248.

Gene expression databases

ArrayExpressP97852.
GermOnlineENSRNOG00000015840. Rattus norvegicus.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR002539. MaoC_deHydtase.
IPR016040. NAD(P)-bd_dom.
IPR003033. SCP2_sterol_bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
PF02036. SCP2. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio614694.

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Entry information

Entry nameDHB4_RAT
AccessionPrimary (citable) accession number: P97852
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 77 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents