- Short-chain dehydrogenase
Pfam_box
Symbol = adh_short
Name = short chain dehydrogenase
width =
caption =
Pfam= PF00106
InterPro= IPR002198
SMART=
PROSITE = PDOC00060
SCOP = 1hdc
TCDB =
OPM family= 127
OPM protein= 1xu7
PDB=PDB3|1edoA:78-246 PDB3|1zbqA:10-183 PDB3|1gz6A:10-183PDB3|1gcoA:8-177 PDB3|1g6kB:8-177 PDB3|1geeF:8-177PDB3|1rwbE:8-177 PDB3|1hxhC:8-171 PDB3|1nfqA:8-172PDB3|1nfrA:8-172 PDB3|1nffB:8-172 PDB3|2hsdA:7-171PDB3|1hdcC:7-171 PDB3|1zk0A:8-163 PDB3|1zk3B:8-163PDB3|1zk4A:8-163 PDB3|1zjzA:8-163 PDB3|1zk1A:8-163PDB3|1zk2A:8-163 PDB3|1zjyA:8-163 PDB3|1nxqA:8-163PDB3|2bglA:17-186 PDB3|2bgkB:17-186 PDB3|2bgmA:17-186PDB3|1iy8D:14-184 PDB3|1k2wA:6-171 PDB3|1uzoA:6-171PDB3|1gegC:3-171 PDB3|1wmbB:5-174 PDB3|1x7gA:7-176PDB3|1w4zB:7-176 PDB3|1xr3A:7-176 PDB3|1x7hA:7-176PDB3|1e3wD:11-187 PDB3|1e3sC:11-187 PDB3|1e6wD:11-187PDB3|1u7tB:11-187 PDB3|1so8A:11-187 PDB3|1f67A:11-187PDB3|1uayA:3-167 PDB3|1yxmB:19-157 PDB3|2ag5D:7-166PDB3|1dohA:30-197 PDB3|1g0nA:30-197 PDB3|1g0oA:30-197PDB3|1ybvA:30-197 PDB3|1ja9A:22-189 PDB3|1vl8A:10-179PDB3|1ydeM:10-173 PDB3|1spxA:7-153 PDB3|1xkqA:7-181PDB3|1xhlB:7-179 PDB3|1wntB:8-168 PDB3|1pr9A:8-168PDB3|1cydB:8-168 PDB3|2bd0C:3-177 PDB3|1h5qL:12-188PDB3|1fdvD:4-175 PDB3|1iol :4-175 PDB3|1fdw :4-175PDB3|3dheA:4-175 PDB3|1fduD:4-175 PDB3|1equA:4-175PDB3|1qywA:4-175 PDB3|1i5rA:4-175 PDB3|1dhtA:4-175PDB3|1qyxA:4-175 PDB3|1fdt :4-175 PDB3|1a27 :4-175PDB3|1bhs :4-175 PDB3|1jtvA:4-175 PDB3|1qyvA:4-175PDB3|1fds :4-175 PDB3|1xg5A:12-185 PDB3|1wmaA:6-144PDB3|1n5dA:6-140 PDB3|1xq1A:15-183 PDB3|1ipeA:10-178PDB3|2ae2A:10-178 PDB3|1ipfB:10-178 PDB3|2ae1 :10-178PDB3|1ae1A:22-190 PDB3|1bdb :6-174 PDB3|1o5iB:8-160PDB3|1yb1B:37-204 PDB3|2belC:35-202 PDB3|1xu7D:35-202PDB3|1xu9D:35-202 PDB3|1y5rA:35-202 PDB3|1y5mA:35-202PDB3|1xseA:35-202 PDB3|2bfmB:7-213 PDB3|1e92A:7-213PDB3|1w0cE:7-213 PDB3|2bfoD:7-213 PDB3|2bf7B:7-213PDB3|2bfpB:7-213 PDB3|2bfaD:7-213 PDB3|1e7wB:7-213PDB3|1p33B:8-214 PDB3|1mxfC:12-201 PDB3|1mxhC:12-201PDB3|1w73D:60-229 PDB3|1w8dB:60-229 PDB3|1snyA:2-188PDB3|1yo6C:4-155 PDB3|1z6zB:8-189 PDB3|1oaa :9-190PDB3|1nasA:9-190 PDB3|1sep :9-190 PDB3|1mg5A:9-172PDB3|1b14B:6-170 PDB3|1sbyB:6-170 PDB3|1a4uB:6-170PDB3|1b15A:6-170 PDB3|1b16B:6-170 PDB3|1b2lA:6-170PDB3|1fk8A:2-129 PDB3|1fjhA:2-129 PDB3|1jvfA:7-177PDB3|1jw7A:7-177 PDB3|1dirD:8-166 PDB3|1dhr :8-166PDB3|1hdr :11-169 PDB3|1ooeB:4-162The short-chain dehydrogenases/reductases family (SDR)cite journal |author=Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D, Jornvall H |title=Short-chain dehydrogenases/reductases (SDR) |journal=Biochemistry |volume=34 |issue=18 |pages=6003–6013 |year=1995 |pmid=7742302 |doi=10.1021/bi00039a038] 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 Drosophilaalcohol dehydrogenase , this family used to be calledcite journal |author=Villarroya A, Juan E, Egestad B, Jornvall H |title=The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc |journal=Eur. J. Biochem. |volume=180 |issue=1 |pages=191–197 |year=1989 |pmid=2707261 |doi=10.1111/j.1432-1033.1989.tb14632.x] cite journal |author=Persson B, Krook M, Jornvall H |title=Characteristics of short-chain alcohol dehydrogenases and related enzymes |journal=Eur. J. Biochem. |volume=200 |issue=2 |pages=537–543 |year=1991 |pmid=1889416 |doi=10.1111/j.1432-1033.1991.tb16215.x] cite journal |author=Harayama S, Bairoch A, Hartnett C, Rekik M, Ornston LN, Neidle E |title=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 |journal=Eur. J. Biochem. |volume=204 |issue=1 |pages=113–120 |year=1992 |pmid=1740120 |doi=10.1111/j.1432-1033.1992.tb16612.x] '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 domainscite journal |author=Benyajati C, Place AR, Powers DA, Sofer W |title=Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue=5 |pages=2717–2721 |year=1981 |pmid=6789320 |doi=10.1073/pnas.78.5.2717] , 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.ubfamilies
*
Glucose/ribitol dehydrogenase InterPro|IPR002347
*Insect alcohol dehydrogenase family InterPro|IPR002424
*2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase InterPro|IPR003560Human 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 ;References
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