ADH2_CAEEL
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 03-AUG-2022, entry version 139.
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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z81570; CAB04603.1; -; Genomic_DNA.
DR PIR; T23625; T23625.
DR RefSeq; NP_505992.1; NM_073591.3.
DR AlphaFoldDB; O45687; -.
DR SMR; O45687; -.
DR BioGRID; 44652; 1.
DR IntAct; O45687; 1.
DR STRING; 6239.K12G11.4; -.
DR PaxDb; O45687; -.
DR PeptideAtlas; O45687; -.
DR EnsemblMetazoa; K12G11.4.1; K12G11.4.1; WBGene00010791.
DR GeneID; 179628; -.
DR KEGG; cel:CELE_K12G11.4; -.
DR UCSC; K12G11.4; c. elegans.
DR CTD; 41313; -.
DR WormBase; K12G11.4; CE12214; WBGene00010791; sodh-2.
DR eggNOG; KOG0023; Eukaryota.
DR GeneTree; ENSGT00940000171159; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; O45687; -.
DR OMA; QYAHNVF; -.
DR OrthoDB; 771875at2759; -.
DR PhylomeDB; O45687; -.
DR PRO; PR:O45687; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010791; Expressed in embryo and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..351
FT /note="Alcohol dehydrogenase 2"
FT /id="PRO_0000160694"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 181..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
