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InterPro: IPR013154 Alcohol dehydrogenase GroES-like

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UniProtKB
Matches:
18557 proteins
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IPR013154 ADH_GroES-like
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Domain
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Parent IPR011032 GroES-like
Found in IPR002085 Alcohol dehydrogenase superfamily, zinc-containing
IPR004627 L-threonine 3-dehydrogenase
IPR005903 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase
IPR010085 Crotonyl-CoA reductase
IPR014182 Alcohol dehydrogenase, zinc-binding type 1
IPR014183 Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
IPR014184 Formaldehyde dehydrogenase, glutathione-independent
IPR014187 Alcohol dehydrogenase, zinc-binding type 2
IPR014188 Quinone oxidoreductase putative, YhdH/YhfP
IPR014189 Quinone oxidoreductase putative, PIG3
IPR017614 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase
IPR017743 Alcohol dehydrogenase, phosphonate catabolism-associated, putative
IPR017816 Formaldehyde dehydrogenase, mycothiol-dependent
IPR020843 Polyketide synthase, enoylreductase
Contains IPR002328 Alcohol dehydrogenase, zinc-containing, conserved site
GO Term annotationHelp
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Function GO:0016491 oxidoreductase activity
InterPro annotation
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AbstractHelp
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This is the catalytic domain of alcohol dehydrogenases (EC:1.1.1.1). Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure; a name derived from the superfamily of proteins with a GroES fold. Proteins with a GroES fold structure have a highly conserved hydrophobic core and a glycyl-aspartate dipeptide which is thought to maintain the fold [1, 2].
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PDB - click here
1a71 , 1a72 , 1adb , 1adc , 1adf , 1adg , 1agn , 1axe , 1axg , 1bto , 1bxz , 1cdo , 1d1s , 1d1t , 1deh , 1e3e , 1e3i , 1e3j , 1e3l , 1ee2 , 1f8f , 1gu7 , 1guf , 1gyr , 1h0k , 1h2b , 1hdx , 1hdy , 1hdz , 1het , 1heu , 1hf3 , 1hld , 1hso , 1hsz , 1ht0 , 1htb , 1iyz , 1iz0 , 1jqb , 1ju9 , 1jvb , 1kev , 1kol , 1lde , 1ldy , 1llu , 1m6h , 1m6w , 1ma0 , 1mc5 , 1mg0 , 1mgo , 1mp0 , 1n8k , 1n92 , 1n9g , 1nto , 1nvg , 1o89 , 1o8c , 1p0c , 1p0f , 1p1r , 1ped , 1piw , 1pl6 , 1pl7 , 1pl8 , 1pqw , 1ps0 , 1q1n , 1qlh , 1qlj , 1qor , 1qv6 , 1qv7 , 1r37 , 1rjw , 1teh , 1tt7 , 1u3t , 1u3u , 1u3v , 1u3w , 1uuf , 1vj0 , 1wly , 1y9a , 1y9e , 1yb5 , 1ye3 , 1ykf , 1yqd , 1yqx , 2b83 , 2cf5 , 2cf6 , 2dph , 2eer , 2fze , 2fzw , 2h6e , 2hcy , 2jhf , 2jhg , 2nvb , 2ohx , 2oui , 2oxi , 3bto , 3cos , 3hud , 5adh , 6adh , 7adh , 8adh
SCOP: b.35.1.2 , c.2.1.1
CATH: 3.90.180.10
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Enzyme: EC:1
Blocks: IPB013154
Pfam Clan: CL0296.1

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Overlapping InterPro entriesHelp
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IPR013154 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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O45687 Alcohol dehydrogenase 2

P00325 Alcohol dehydrogenase 1B

P00330 Alcohol dehydrogenase 1

P46415 Alcohol dehydrogenase class-3

Q9QYY9 Alcohol dehydrogenase 4

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002328 Alcohol dehydrogenase, zinc-containing, conserved site
IPR013149 Alcohol dehydrogenase, zinc-binding
IPR013154 Alcohol dehydrogenase GroES-like
IPR011032 GroES-like
IPR016040 NAD(P)-binding domain
IPR002085 Alcohol dehydrogenase superfamily, zinc-containing
IPR014183 Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
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1. Taneja B, Mande SC.
Conserved structural features and sequence patterns in the GroES fold family.
Protein Eng. 12 815-8 1999 [PubMed: 10556240]
http://dx.doi.org/10.1093/protein/12.10.815
2. Murzin AG.
Structural classification of proteins: new superfamilies.
Curr. Opin. Struct. Biol. 6 386-94 1996 [PubMed: 8804825]
http://dx.doi.org/10.1016/S0959-440X(96)80059-5

Additional ReadingHelp
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Goihberg E, Dym O, Tel-Or S, Shimon L, Frolow F, Peretz M, Burstein Y.
Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution.
Proteins 72 2008 711-9 [PubMed: 18260103]
http://dx.doi.org/10.1002/prot.21946
Youn B, Camacho R, Moinuddin SG, Lee C, Davin LB, Lewis NG, Kang C.
Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4.
Org. Biomol. Chem. 4 2006 1687-97 [PubMed: 16633561]
http://dx.doi.org/10.1039/b601672c
Brouns SJ, Turnbull AP, Willemen HL, Akerboom J, van der Oost J.
Crystal structure and biochemical properties of the D-arabinose dehydrogenase from Sulfolobus solfataricus.
J. Mol. Biol. 371 2007 1249-60 [PubMed: 17610898]
http://dx.doi.org/10.1016/j.jmb.2007.05.097
Meijers R, Adolph HW, Dauter Z, Wilson KS, Lamzin VS, Cedergren-Zeppezauer ES.
Structural evidence for a ligand coordination switch in liver alcohol dehydrogenase.
Biochemistry 46 2007 5446-54 [PubMed: 17429946]
http://dx.doi.org/10.1021/bi6023594
Goihberg E, Dym O, Tel-Or S, Levin I, Peretz M, Burstein Y.
A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase.
Proteins 66 2007 196-204 [PubMed: 17063493]
http://dx.doi.org/10.1002/prot.21170
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