ID ADHX_ORYSJ Reviewed; 381 AA. AC Q0DWH1; P93436; Q6K6C1; DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 23. DE RecName: Full=Alcohol dehydrogenase class-3; DE EC=1.1.1.1; DE AltName: Full=Alcohol dehydrogenase class-III; DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase; DE EC=1.1.1.284; DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase; DE Short=GSH-FDH; DE Short=FALDH; DE Short=FDH; DE EC=1.1.1.-; GN OrderedLocusNames=Os02g0815500, LOC_Os02g57040; GN ORFNames=P0643F09.4, OsJ_008550; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=17210932; DOI=10.1101/gr.5509507; RG The rice annotation project (RAP); RT "Curated genome annotation of Oryza sativa ssp. japonica and RT comparative genome analysis with Arabidopsis thaliana."; RL Genome Res. 17:175-183(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., RA Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., RA Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., RA Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., RA Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., RA Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., RA Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., RA Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., RA Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., RA Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., RA Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., RA Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX MEDLINE=22752273; PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone + CC NADH. CC -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S- CC formylglutathione + NAD(P)H. CC -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-III subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP004120; BAD21676.1; -; Genomic_DNA. DR EMBL; AP005111; BAD21999.1; -; Genomic_DNA. DR EMBL; AP008208; BAF10417.1; -; Genomic_DNA. DR EMBL; CM000139; EAZ25067.1; -; Genomic_DNA. DR EMBL; AK099733; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; NP_001048503.1; -. DR UniGene; Os.59290; -. DR HSSP; P11766; 1M6H. DR GeneID; 4331130; -. DR KEGG; osa:4331130; -. DR Gramene; P93436; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC. DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase ...; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR014183; ADH_3. DR InterPro; IPR013154; ADH_GroES-like. DR InterPro; IPR002085; ADH_SF_Zn. DR InterPro; IPR013149; ADH_Zn-bd. DR InterPro; IPR002328; ADH_Zn_CS. DR PANTHER; PTHR11695; ADH_Sf_Zn; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc. FT CHAIN 1 381 Alcohol dehydrogenase class-3. FT /FTId=PRO_0000160773. FT METAL 49 49 Zinc 1; catalytic (By similarity). FT METAL 71 71 Zinc 1; catalytic (By similarity). FT METAL 101 101 Zinc 2 (By similarity). FT METAL 104 104 Zinc 2 (By similarity). FT METAL 107 107 Zinc 2 (By similarity). FT METAL 115 115 Zinc 2 (By similarity). FT METAL 179 179 Zinc 1; catalytic (By similarity). FT CONFLICT 318 318 V -> I (in Ref. 4; AK099733). SQ SEQUENCE 381 AA; 40823 MW; C107E6B8B2CB7F58 CRC64; MASSTQGQVI TCKAAVAWEA NRPMTIEDVQ VAPPQAGEVR VKILFTALCH TDHYTWSGKD PEGLFPCILG HEAAGIVESV GEGVTEVQPG DHVIPCYQAE CRECKFCKSG KTNLCGKVRA ATGVGVMMND RKSRFSINGK PIYHFMGTST FSQYTVVHDV SVAKINPQAP LDKVCLLGCG VSTGLGAVWN TAKVEAGSIV AIFGLGTVGL AVAEGAKSAG ASRIIGIDID SKKFDVAKNF GVTEFVNPKD HDKPIQQVIV DLTDGGVDYS FECIGNVSVM RSALECCHKG WGTSVIVGVA ASGQEISTRP FQLVTGRVWK GTAFGGFKSR SQVPWLVEKY LNKEIKVDEY VTHSMNLTDI NKAFDLLHEG GCLRCVLATD K //