ID   ADH2_CAEEL              Reviewed;         351 AA.
AC   O45687;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Alcohol dehydrogenase 2;
DE            EC=1.1.1.1;
DE   AltName: Full=Sorbitol dehydrogenase family protein 2;
GN   Name=sodh-2; ORFNames=K12G11.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (Potential).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family.
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DR   EMBL; Z81570; CAB04603.1; -; Genomic_DNA.
DR   PIR; T23625; T23625.
DR   RefSeq; NP_505992.1; -.
DR   UniGene; Cel.2991; -.
DR   Ensembl; K12G11.4; Caenorhabditis elegans.
DR   GeneID; 179628; -.
DR   KEGG; cel:K12G11.4; -.
DR   NMPDR; fig|6239.3.peg.19849; -.
DR   WormBase; WBGene00010791; sodh-2.
DR   WormPep; K12G11.4; CE12214.
DR   OMA; O45687; LINANCL.
DR   BRENDA; 1.1.1.1; 672.
DR   NextBio; 906206; -.
DR   ArrayExpress; O45687; -.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008340; P:determination of adult life span; IMP:WormBase.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN         1    351       Alcohol dehydrogenase 2.
FT                                /FTId=PRO_0000160694.
FT   NP_BIND     181    187       NAD (By similarity).
FT   NP_BIND     271    273       NAD (By similarity).
FT   METAL        47     47       Zinc 1; catalytic (By similarity).
FT   METAL        70     70       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       157    157       Zinc 1; catalytic (By similarity).
FT   BINDING     205    205       NAD (By similarity).
FT   BINDING     209    209       NAD (By similarity).
FT   BINDING     343    343       NAD (By similarity).
SQ   SEQUENCE   351 AA;  37945 MW;  D806D1DA6AB9AEEB CRC64;
     MSSANIPATQ SALIFEKYGG PLEVRQVSVP QPQENELLVK IEYSGICHSD LHTWEGDFEY
     ASICPLIGGH EGAGTVVTIG SKVKGWNIGD RAGIKLINAN CLNCEYCKTG HEPLCDHIQN
     YGIDRHGTFQ EYLTIRDIDA IKVSNDTNLA AAAPVLCGGV TAYKSLKATN VKPGQIVVLT
     GAGGGLGSFG IQYAKAMGMR VVAVDHISKE DHCRNLGAEW FVDAFDTPDI VAHIRKLTNG
     GAHGVVSFAA AKKPMEYALE YVRKRGTVVF VGLPKDGTIP LDTLSLICNE ITVKGSIVGS
     RMDVDEAIDF ITRGIVHVPI ELVKLEDVPS VYQRMKDGKV TSRVVVDFSM R
//