Summary: short chain dehydrogenase
This is the Wikipedia entry entitled "Short-chain dehydrogenase". More...
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Short-chain dehydrogenase Edit Wikipedia article
|short chain dehydrogenase|
The short-chain dehydrogenases/reductases family (SDR) is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called 'insect-type', or 'short-chain' alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains, the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains.
- Glucose/ribitol dehydrogenase IPR002347
- Insect alcohol dehydrogenase family IPR002424
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase IPR003560
Human proteins containing this domain
17BHSDI; BDH1; BDH2; CBR1; CBR3; CBR4; DCXR; DECR1; DECR2; DHRS1; DHRS10; DHRS13; DHRS2; DHRS3; DHRS4; DHRS4L2; DHRS7; DHRS7B; DHRS8; DHRS9; DHRSX; FASN; FVT1; HADH2; HPGD; HSD11B1; HSD11B2; HSD17B1; HSD17B10; HSD17B12; HSD17B13; HSD17B2; HSD17B3; HSD17B4; HSD17B6; HSD17B7; HSD17B7P2; HSD17B8; HSDL1; HSDL2; PECR; QDPR; RDH10; RDH11; RDH12; RDH13; RDH14; RDH16; RDH5; RDH8; RDHE2; RDHS; SCDR10; SPR; WWOX;
- Ghosh D, Erman M, Wawrzak Z, Duax WL, Pangborn W (October 1994). "Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor". Structure 2 (10): 973–80. doi:10.1016/S0969-2126(94)00099-9. PMID 7866748.
- Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D, Jornvall H (1995). "Short-chain dehydrogenases/reductases (SDR)". Biochemistry 34 (18): 6003–6013. doi:10.1021/bi00039a038. PMID 7742302.
- Villarroya A, Juan E, Egestad B, Jornvall H (1989). "The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc". Eur. J. Biochem. 180 (1): 191–197. doi:10.1111/j.1432-1033.1989.tb14632.x. PMID 2707261.
- Persson B, Krook M, Jornvall H (1991). "Characteristics of short-chain alcohol dehydrogenases and related enzymes". Eur. J. Biochem. 200 (2): 537–543. doi:10.1111/j.1432-1033.1991.tb16215.x. PMID 1889416.
- Harayama S, Bairoch A, Hartnett C, Rekik M, Ornston LN, Neidle E (1992). "cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily". Eur. J. Biochem. 204 (1): 113–120. doi:10.1111/j.1432-1033.1992.tb16612.x. PMID 1740120.
- Benyajati C, Place AR, Powers DA, Sofer W (1981). "Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein". Proc. Natl. Acad. Sci. U.S.A. 78 (5): 2717–2721. doi:10.1073/pnas.78.5.2717. PMC 319428. PMID 6789320.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
short chain dehydrogenase Provide feedback
This family contains a wide variety of dehydrogenases.
Benach J, Atrian S, Gonzalez-Duarte R, Ladenstein R; , J Mol Biol 1998;282:383-399.: The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution. PUBMED:9735295 EPMC:9735295
Yamashita A, Kato H, Wakatsuki S, Tomizaki T, Nakatsu T, Nakajima K, Hashimoto T, Yamada Y, Oda J; , Biochemistry 1999;38:7630-7637.: Structure of tropinone reductase-II complexed with NADP+ and pseudotropine at 1.9 A resolution: implication for stereospecific substrate binding and catalysis. PUBMED:10387002 EPMC:10387002
Internal database links
|Similarity to PfamA using HHSearch:||3Beta_HSD Saccharop_dh Epimerase Polysacc_synt_2 RmlD_sub_bind Shikimate_DH NAD_binding_4 KR NAD_binding_10 adh_short_C2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002198The short-chain dehydrogenases/reductases family (SDR) [PUBMED:7742302] is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called [PUBMED:2707261, PUBMED:1889416, PUBMED:1740120] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most member of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains [PUBMED:6789320], the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains [PUBMED:6789320].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||oxidoreductase activity (GO:0016491)|
|Biological process||metabolic process (GO:0008152)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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A class of redox enzymes are two domain proteins. One domain, termed the catalytic domain, confers substrate specificity and the precise reaction of the enzyme. The other domain, which is common to this class of redox enzymes, is a Rossmann-fold domain. The Rossmann domain binds nicotinamide adenine dinucleotide (NAD+) and it is this cofactor that reversibly accepts a hydride ion, which is lost or gained by the substrate in the redox reaction. Rossmann domains have an alpha/beta fold, which has a central beta sheet, with approximately five alpha helices found surrounding the beta sheet.The strands forming the beta sheet are found in the following characteristic order 654123. The inter sheet crossover of the stands in the sheet form the NAD+ binding site . In some more distantly relate Rossmann domains the NAD+ cofactor is replaced by the functionally similar cofactor FAD.
The clan contains the following 180 members:2-Hacid_dh_C 3Beta_HSD 3HCDH_N adh_short adh_short_C2 ADH_zinc_N ADH_zinc_N_2 AdoHcyase_NAD AdoMet_MTase AlaDh_PNT_C Amino_oxidase ApbA AviRa Bac_GDH Bin3 CheR CMAS CmcI CoA_binding CoA_binding_2 CoA_binding_3 Cons_hypoth95 DAO DapB_N DFP DNA_circ_N DNA_methylase DOT1 DREV dTMP_synthase DUF1442 DUF1776 DUF2431 DUF268 DUF3321 DUF43 DUF633 DUF938 DXP_redisom_C DXP_reductoisom Eco57I ELFV_dehydrog Eno-Rase_FAD_bd Eno-Rase_NADH_b Enoyl_reductase Epimerase F420_oxidored FAD_binding_2 FAD_binding_3 FAD_oxidored Fibrillarin FMO-like FmrO FtsJ G-7-MTase G6PD_N GCD14 GDI GFO_IDH_MocA GIDA GidB GLF Glyco_hydro_4 GMC_oxred_N Gp_dh_N GRAS GRDA HI0933_like HIM1 IlvN K_oxygenase KR LCM Ldh_1_N Lycopene_cycl Malic_M Mannitol_dh Met_10 Methyltrans_Mon Methyltrans_SAM Methyltransf_10 Methyltransf_11 Methyltransf_12 Methyltransf_15 Methyltransf_16 Methyltransf_17 Methyltransf_18 Methyltransf_19 Methyltransf_2 Methyltransf_20 Methyltransf_21 Methyltransf_22 Methyltransf_23 Methyltransf_24 Methyltransf_25 Methyltransf_26 Methyltransf_27 Methyltransf_28 Methyltransf_29 Methyltransf_3 Methyltransf_30 Methyltransf_31 Methyltransf_32 Methyltransf_4 Methyltransf_5 Methyltransf_7 Methyltransf_8 Methyltransf_9 Methyltransf_PK MethyltransfD12 MetW Mg-por_mtran_C Mqo MT-A70 MTS Mur_ligase N2227 N6-adenineMlase N6_Mtase N6_N4_Mtase NAD_binding_10 NAD_binding_11 NAD_binding_2 NAD_binding_3 NAD_binding_4 NAD_binding_5 NAD_binding_7 NAD_binding_8 NAD_binding_9 NAD_Gly3P_dh_N NAS NmrA NNMT_PNMT_TEMT NodS Nol1_Nop2_Fmu Nol1_Nop2_Fmu_2 NSP13 OCD_Mu_crystall PARP_regulatory PCMT PDH Polysacc_synt_2 Pox_MCEL Prenylcys_lyase PrmA PRMT5 Pyr_redox Pyr_redox_2 Pyr_redox_3 RmlD_sub_bind Rossmann-like rRNA_methylase RrnaAD Rsm22 RsmJ Saccharop_dh SAM_MT SE Semialdhyde_dh Shikimate_DH Spermine_synth Strep_67kDa_ant TehB THF_DHG_CYH_C Thi4 ThiF TPMT TrkA_N TRM TRM13 tRNA_U5-meth_tr Trp_halogenase TylF Ubie_methyltran UDPG_MGDP_dh_N UPF0020 UPF0146 V_cholerae_RfbT XdhC_C YjeF_N
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Author:||Sonnhammer ELL, Griffiths-Jones SR|
|Number in seed:||230|
|Number in full:||80936|
|Average length of the domain:||163.30 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||56.70 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||20|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the adh_short domain has been found. There are 916 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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