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Protein

3-hydroxybutyrate dehydrogenase type 2

Gene

BDH2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Dehydrogenase that mediates the formation of 2,5-dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural similarities with bacterial enterobactin and associates with LCN2, thereby playing a key role in iron homeostasis and transport. Also acts as a 3-hydroxybutyrate dehydrogenase (By similarity).By similarity1 Publication

Catalytic activityi

(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH.

Kineticsi

  1. KM=60 µM for NAD1 Publication
  2. KM=10 mM for R-hydroxybutyrate1 Publication
  1. Vmax=82 nmol/min/mg enzyme (at 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.5-9.0.1 Publication

Pathwayi: Siderophore biosynthesis

This protein is involved in Siderophore biosynthesis.
View all proteins of this organism that are known to be involved in Siderophore biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581NAD1 Publication
Binding sitei144 – 1441SubstrateCurated
Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation
Binding sitei151 – 1511NAD1 Publication
Binding sitei188 – 1881SubstrateCurated
Binding sitei205 – 2051SubstrateCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 3728NAD1 PublicationAdd
BLAST
Nucleotide bindingi180 – 1845NAD1 Publication

GO - Molecular functioni

  • 3-hydroxybutyrate dehydrogenase activity Source: HGNC
  • NAD binding Source: HGNC
  • oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS08987-MONOMER.
ReactomeiR-HSA-77111. Synthesis of Ketone Bodies.
SABIO-RKQ9BUT1.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxybutyrate dehydrogenase type 2 (EC:1.1.1.-, EC:1.1.1.30)
Alternative name(s):
Dehydrogenase/reductase SDR family member 6
Oxidoreductase UCPA
R-beta-hydroxybutyrate dehydrogenase
Short chain dehydrogenase/reductase family 15C member 1
Gene namesi
Name:BDH2
Synonyms:DHRS6, SDR15C1
ORF Names:UNQ6308/PRO20933
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:32389. BDH2.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672559.

Polymorphism and mutation databases

BioMutaiBDH2.
DMDMi125987797.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2452453-hydroxybutyrate dehydrogenase type 2PRO_0000042580Add
BLAST

Proteomic databases

EPDiQ9BUT1.
MaxQBiQ9BUT1.
PaxDbiQ9BUT1.
PeptideAtlasiQ9BUT1.
PRIDEiQ9BUT1.

PTM databases

iPTMnetiQ9BUT1.
PhosphoSiteiQ9BUT1.

Expressioni

Gene expression databases

BgeeiQ9BUT1.
CleanExiHS_BDH2.
ExpressionAtlasiQ9BUT1. baseline and differential.
GenevisibleiQ9BUT1. HS.

Organism-specific databases

HPAiHPA036028.
HPA036029.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi121228. 10 interactions.
STRINGi9606.ENSP00000296424.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Beta strandi8 – 136Combined sources
Helixi17 – 2812Combined sources
Beta strandi32 – 387Combined sources
Helixi40 – 434Combined sources
Helixi44 – 485Combined sources
Beta strandi52 – 565Combined sources
Helixi62 – 7110Combined sources
Beta strandi76 – 805Combined sources
Helixi90 – 923Combined sources
Helixi95 – 10511Combined sources
Helixi107 – 12317Combined sources
Beta strandi126 – 1316Combined sources
Turni136 – 1383Combined sources
Helixi145 – 16521Combined sources
Helixi166 – 1683Combined sources
Beta strandi170 – 1789Combined sources
Helixi183 – 1919Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 20410Combined sources
Helixi214 – 22512Combined sources
Helixi227 – 2293Combined sources
Beta strandi236 – 2394Combined sources
Helixi243 – 2453Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AG5X-ray1.84A/B/C/D1-245[»]
ProteinModelPortaliQ9BUT1.
SMRiQ9BUT1. Positions 1-245.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BUT1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG002145.
InParanoidiQ9BUT1.
KOiK00019.
OMAiTHETPRI.
OrthoDBiEOG7W154W.
PhylomeDBiQ9BUT1.
TreeFamiTF328795.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BUT1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP
60 70 80 90 100
GIQTRVLDVT KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF
110 120 130 140 150
SMNLNVRSMY LMIKAFLPKM LAQKSGNIIN MSSVASSVKG VVNRCVYSTT
160 170 180 190 200
KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARGNPEEARN
210 220 230 240
DFLKRQKTGR FATAEEIAML CVYLASDESA YVTGNPVIID GGWSL
Length:245
Mass (Da):26,724
Last modified:February 6, 2007 - v2
Checksum:iA6E10E9DF9304107
GO
Isoform 2 (identifier: Q9BUT1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-245: VVNRCVYSTT...PVIIDGGWSL → GSVSFRGLRCSYTHIIKSSAFGNRHSRDYNFKY

Show »
Length:173
Mass (Da):19,209
Checksum:i23BD76240A349C5F
GO
Isoform 3 (identifier: Q9BUT1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Show »
Length:144
Mass (Da):15,626
Checksum:i84FAF6A1B536C6B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951E → V in BAF82849 (PubMed:14702039).Curated
Sequence conflicti161 – 1611V → L in AAQ89200 (PubMed:12975309).Curated
Sequence conflicti203 – 2031L → P in BAF82849 (PubMed:14702039).Curated
Sequence conflicti230 – 2301A → T in AAH95414 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti70 – 701N → S.4 Publications
Corresponds to variant rs1054707 [ dbSNP | Ensembl ].
VAR_023602

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 101101Missing in isoform 3. 1 PublicationVSP_039781Add
BLAST
Alternative sequencei141 – 245105VVNRC…GGWSL → GSVSFRGLRCSYTHIIKSSA FGNRHSRDYNFKY in isoform 2. 3 PublicationsVSP_015859Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164790 mRNA. Translation: AAF80754.1.
AY358841 mRNA. Translation: AAQ89200.1.
CR457309 mRNA. Translation: CAG33590.1.
AK023323 mRNA. Translation: BAB14526.1.
AK290160 mRNA. Translation: BAF82849.1.
AK300626 mRNA. Translation: BAG62318.1.
AC097485 Genomic DNA. No translation available.
BC037277 mRNA. Translation: AAH37277.1.
BC001953 mRNA. Translation: AAH01953.1.
BC095414 mRNA. Translation: AAH95414.1.
CCDSiCCDS3663.1. [Q9BUT1-1]
RefSeqiNP_064524.3. NM_020139.3. [Q9BUT1-1]
XP_011530430.1. XM_011532128.1. [Q9BUT1-1]
UniGeneiHs.124696.

Genome annotation databases

EnsembliENST00000296424; ENSP00000296424; ENSG00000164039. [Q9BUT1-1]
GeneIDi56898.
KEGGihsa:56898.
UCSCiuc003hwz.4. human. [Q9BUT1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164790 mRNA. Translation: AAF80754.1.
AY358841 mRNA. Translation: AAQ89200.1.
CR457309 mRNA. Translation: CAG33590.1.
AK023323 mRNA. Translation: BAB14526.1.
AK290160 mRNA. Translation: BAF82849.1.
AK300626 mRNA. Translation: BAG62318.1.
AC097485 Genomic DNA. No translation available.
BC037277 mRNA. Translation: AAH37277.1.
BC001953 mRNA. Translation: AAH01953.1.
BC095414 mRNA. Translation: AAH95414.1.
CCDSiCCDS3663.1. [Q9BUT1-1]
RefSeqiNP_064524.3. NM_020139.3. [Q9BUT1-1]
XP_011530430.1. XM_011532128.1. [Q9BUT1-1]
UniGeneiHs.124696.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AG5X-ray1.84A/B/C/D1-245[»]
ProteinModelPortaliQ9BUT1.
SMRiQ9BUT1. Positions 1-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121228. 10 interactions.
STRINGi9606.ENSP00000296424.

PTM databases

iPTMnetiQ9BUT1.
PhosphoSiteiQ9BUT1.

Polymorphism and mutation databases

BioMutaiBDH2.
DMDMi125987797.

Proteomic databases

EPDiQ9BUT1.
MaxQBiQ9BUT1.
PaxDbiQ9BUT1.
PeptideAtlasiQ9BUT1.
PRIDEiQ9BUT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296424; ENSP00000296424; ENSG00000164039. [Q9BUT1-1]
GeneIDi56898.
KEGGihsa:56898.
UCSCiuc003hwz.4. human. [Q9BUT1-1]

Organism-specific databases

CTDi56898.
GeneCardsiBDH2.
H-InvDBHIX0032960.
HGNCiHGNC:32389. BDH2.
HPAiHPA036028.
HPA036029.
neXtProtiNX_Q9BUT1.
PharmGKBiPA142672559.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0725. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG002145.
InParanoidiQ9BUT1.
KOiK00019.
OMAiTHETPRI.
OrthoDBiEOG7W154W.
PhylomeDBiQ9BUT1.
TreeFamiTF328795.

Enzyme and pathway databases

BioCyciMetaCyc:HS08987-MONOMER.
ReactomeiR-HSA-77111. Synthesis of Ketone Bodies.
SABIO-RKQ9BUT1.

Miscellaneous databases

EvolutionaryTraceiQ9BUT1.
GenomeRNAii56898.
PROiQ9BUT1.

Gene expression databases

BgeeiQ9BUT1.
CleanExiHS_BDH2.
ExpressionAtlasiQ9BUT1. baseline and differential.
GenevisibleiQ9BUT1. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hypothalamus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-70.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-70.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT SER-70.
    Tissue: Ovary and Thalamus.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1; 2 AND 3), VARIANT SER-70.
    Tissue: Brain and Skin.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
    Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
    J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.

Entry informationi

Entry nameiBDH2_HUMAN
AccessioniPrimary (citable) accession number: Q9BUT1
Secondary accession number(s): A8K295
, B4DUF6, Q503A0, Q6IA46, Q6UWD3, Q9H8S8, Q9NRX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: February 6, 2007
Last modified: July 6, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.