ADH1_CAEEL
ID ADH1_CAEEL Reviewed; 349 AA.
AC Q17334; O45688;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Alcohol dehydrogenase 1;
DE EC=1.1.1.1;
DE AltName: Full=Sorbitol dehydrogenase family protein 1;
GN Name=sodh-1; ORFNames=K12G11.3;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-349.
RX PubMed=7608988; DOI=10.1007/bf00174040;
RA Glasner J.D., Kocher T.D., Collins J.J.;
RT "Caenorhabditis elegans contains genes encoding two new members of the Zn-
RT containing alcohol dehydrogenase family.";
RL J. Mol. Evol. 41:46-53(1995).
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; CAB04604.1; -; Genomic_DNA.
DR EMBL; U18780; AAB03373.1; -; mRNA.
DR PIR; T23626; T23626.
DR RefSeq; NP_505991.1; NM_073590.5.
DR AlphaFoldDB; Q17334; -.
DR SMR; Q17334; -.
DR BioGRID; 44651; 26.
DR DIP; DIP-26303N; -.
DR IntAct; Q17334; 3.
DR MINT; Q17334; -.
DR STRING; 6239.K12G11.3; -.
DR iPTMnet; Q17334; -.
DR World-2DPAGE; 0011:Q17334; -.
DR World-2DPAGE; 0020:Q17334; -.
DR EPD; Q17334; -.
DR PaxDb; Q17334; -.
DR PeptideAtlas; Q17334; -.
DR EnsemblMetazoa; K12G11.3.1; K12G11.3.1; WBGene00010790.
DR GeneID; 179627; -.
DR KEGG; cel:CELE_K12G11.3; -.
DR UCSC; K12G11.3; c. elegans.
DR CTD; 40836; -.
DR WormBase; K12G11.3; CE12212; WBGene00010790; sodh-1.
DR eggNOG; KOG0023; Eukaryota.
DR GeneTree; ENSGT00940000171159; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; Q17334; -.
DR OMA; GLKMTDT; -.
DR OrthoDB; 771875at2759; -.
DR PhylomeDB; Q17334; -.
DR PRO; PR:Q17334; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010790; Expressed in larva and 4 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 GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..349
FT /note="Alcohol dehydrogenase 1"
FT /id="PRO_0000160693"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 180..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 111..112
FT /note="EP -> DA (in Ref. 2; AAB03373)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> R (in Ref. 2; AAB03373)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> G (in Ref. 2; AAB03373)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="M -> I (in Ref. 2; AAB03373)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="V -> G (in Ref. 2; AAB03373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 37697 MW; 94B2752CFCAC977E CRC64;
MTVELPSTQR ALVFDTWNGP LEVRQVPVPS PADDEILVKI EYSGICHSDL HVWLGDLKDM
SVCPLVGGHE GAGSVVQIGK NVTGWQLGDK AGVKLMNFNC LNCEFCKKGH EPLCHHIQNY
GFDRSGTFQE YLTIRGVDAA KINKDTNLAA AAPILCAGVT VYKALKESNV APGQIIVLTG
AGGGLGSLAI QYACAMGMRV VAMDHGSKEA HCKGLGAEWF VDAFETPDIV SHITKLTEGG
PHGVINFAVA RKPMEQAVEY VRKRGTVVFV GLPKDSKVTF DTTPFIFNAI TIKGSIVGSR
LDVDEAMEFV TRGIVKVPLE LVKLEDVPAV YQRMLDGKIN SRAVVDFSL
