ID   ADHX_BOVIN              Reviewed;         374 AA.
AC   Q3ZC42;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=Alcohol dehydrogenase class-3;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase class-III;
DE   AltName: Full=Alcohol dehydrogenase 5;
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   Name=ADH5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing
CC       ethanol, but it readily catalyzes the oxidation of long-chain
CC       primary alcohols and the oxidation of S-(hydroxymethyl)
CC       glutathione (By similarity).
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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily.
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DR   EMBL; BC102926; AAI02927.1; -; mRNA.
DR   IPI; IPI00692275; -.
DR   RefSeq; NP_001029421.1; -.
DR   UniGene; Bt.49339; -.
DR   SMR; Q3ZC42; 2-374.
DR   Ensembl; ENSBTAG00000016007; Bos taurus.
DR   GeneID; 505515; -.
DR   KEGG; bta:505515; -.
DR   HOVERGEN; Q3ZC42; -.
DR   BRENDA; 1.1.1.1; 251.
DR   BRENDA; 1.1.1.284; 251.
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   Acetylation; Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    374       Alcohol dehydrogenase class-3.
FT                                /FTId=PRO_0000282937.
FT   METAL        45     45       Zinc 1; catalytic (By similarity).
FT   METAL        67     67       Zinc 1; catalytic (By similarity).
FT   METAL        97     97       Zinc 2 (By similarity).
FT   METAL       100    100       Zinc 2 (By similarity).
FT   METAL       103    103       Zinc 2 (By similarity).
FT   METAL       111    111       Zinc 2 (By similarity).
FT   METAL       174    174       Zinc 1; catalytic (By similarity).
FT   SITE        115    115       Important for FDH activity and activation
FT                                by fatty acids (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   374 AA;  39677 MW;  307A47ECEC560C0F CRC64;
     MANQVIKCKA AVAWEAGKPL SIEEVEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGN
     YPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK
     GLMPDGTSRF TCKGKTILHY MGTSTFSEYT VVADISVAKI DPLAPLDKVC LLGCGISTGY
     GAALNAAKVE PGSTCAVFGL GGVGLAVIMG CKMAGAARII GVDINKDKFA RAKEFGASEC
     INPQDFSKPI QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGISV VVGVAASGEE
     IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHSL PFDQINEAFD
     LMHAGKSIRT VVKL
//