ADHX_CAEEL
ID ADHX_CAEEL Reviewed; 384 AA.
AC Q17335; Q8WSP4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Alcohol dehydrogenase class-3;
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P11766};
DE AltName: Full=Alcohol dehydrogenase class-III;
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE Short=FALDH;
DE Short=FDH;
DE Short=GSH-FDH;
DE EC=1.1.1.-;
DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE EC=1.1.1.284 {ECO:0000250|UniProtKB:P11766};
GN ORFNames=H24K24.3;
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 [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
RP FUNCTION, AND MUTAGENESIS OF 120-SER--ILE-384.
RX PubMed=30014846; DOI=10.7554/elife.36833;
RA Hao Y., Yang W., Ren J., Hall Q., Zhang Y., Kaplan J.M.;
RT "Thioredoxin shapes the C. elegans sensory response to Pseudomonas produced
RT nitric oxide.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing ethanol,
CC but it readily catalyzes the oxidation of long-chain primary alcohols
CC and the oxidation of S-(hydroxymethyl) glutathione (By similarity).
CC Plays a role in the calcium flux to the cytoplasm in the ASJ sensory
CC neurons upon removal of a nitric oxide stimulus (PubMed:30014846).
CC {ECO:0000250|UniProtKB:P11766, ECO:0000269|PubMed:30014846}.
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 Evidence={ECO:0000250|UniProtKB:P11766};
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 Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58758; EC=1.1.1.284;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11766}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q17335-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q17335-2; Sequence=VSP_000208;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR EMBL; U18781; AAB03374.1; -; mRNA.
DR EMBL; FO081563; CCD72435.1; -; Genomic_DNA.
DR EMBL; FO081563; CCD72436.1; -; Genomic_DNA.
DR RefSeq; NP_001024016.1; NM_001028845.3. [Q17335-2]
DR RefSeq; NP_741507.1; NM_171434.5. [Q17335-1]
DR AlphaFoldDB; Q17335; -.
DR SMR; Q17335; -.
DR BioGRID; 43670; 28.
DR STRING; 6239.H24K24.3b.1; -.
DR EPD; Q17335; -.
DR PaxDb; Q17335; -.
DR PeptideAtlas; Q17335; -.
DR EnsemblMetazoa; H24K24.3a.1; H24K24.3a.1; WBGene00019240. [Q17335-1]
DR EnsemblMetazoa; H24K24.3b.1; H24K24.3b.1; WBGene00019240. [Q17335-2]
DR GeneID; 178597; -.
DR KEGG; cel:CELE_H24K24.3; -.
DR UCSC; H24K24.3a.1; c. elegans. [Q17335-1]
DR CTD; 178597; -.
DR WormBase; H24K24.3a; CE23822; WBGene00019240; -. [Q17335-1]
DR WormBase; H24K24.3b; CE29978; WBGene00019240; -. [Q17335-2]
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000164379; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q17335; -.
DR OMA; IHHYMGT; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; Q17335; -.
DR Reactome; R-CEL-2161541; Abacavir metabolism.
DR Reactome; R-CEL-5365859; RA biosynthesis pathway.
DR Reactome; R-CEL-71384; Ethanol oxidation.
DR PRO; PR:Q17335; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019240; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006066; P:alcohol metabolic process; NAS:UniProtKB.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR CDD; cd08300; alcohol_DH_class_III; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR014183; ADH_3.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..384
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000160770"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
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|UniProtKB:P11766"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT VAR_SEQ 41
FT /note="K -> KFQ (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000208"
FT MUTAGEN 120..384
FT /note="Missing: In nu518; diminishes the calcium flux to
FT the cytoplasm in the ASJ sensory neurons upon removal of a
FT nitric oxide stimulus."
FT /evidence="ECO:0000269|PubMed:30014846"
SQ SEQUENCE 384 AA; 41292 MW; E7FA7F7D55CD3908 CRC64;
MSSTAGQVIN CKAAVAWSAK APLSIETIQV APPKAHEVRV KILYTAVCHT DAYTLDGHDP
EGLFPVVLGH EGSGIVESVG EGVTGFAPGD HVVPLYVPQC KECEYCKNPK TNLCQKIRIS
QGNGFMPDGS SRFTCNGKQL FHFMGCSTFS EYTVVADISL CKVNPEAPLE KVSLLGCGIS
TGYGAVLNTC KVEEGSTVAV WGLGAVGLAV IMGAKAAGAK KIVGIDLIES KFESAKFFGA
TECINPKSVE LPEGKSFQAW LVEQFDGGFD YTFECIGNVH TMRQALEAAH KGWGVSCIIG
VAGAGQEIAT RPFQLVTGRT WKGTAFGGWK SVESVPRLVD DYMNKKLLID EFITHRWNID
DINTAFDVLH KGESLRSVLA FEKI
