ADHX_DROME
ID ADHX_DROME Reviewed; 379 AA.
AC P46415; Q9VGV2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Alcohol dehydrogenase class-3;
DE EC=1.1.1.1 {ECO:0000269|PubMed:8197167};
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=Octanol dehydrogenase;
DE EC=1.1.1.73 {ECO:0000269|PubMed:8197167};
DE AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE EC=1.1.1.284 {ECO:0000269|PubMed:8197167};
GN Name=Fdh; Synonyms=gfd, ODH; ORFNames=CG6598;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7957234; DOI=10.1111/j.1432-1033.1994.0985b.x;
RA Luque T., Atrian S., Danielsson O., Joernvall H., Gonzalez-Duarte R.;
RT "Structure of the Drosophila melanogaster glutathione-dependent
RT formaldehyde dehydrogenase/octanol dehydrogenase gene (class III alcohol
RT dehydrogenase). Evolutionary pathway of the alcohol dehydrogenase genes.";
RL Eur. J. Biochem. 225:985-993(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT
RP SER-2, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8197167; DOI=10.1073/pnas.91.11.4980;
RA Danielsson O., Atrian S., Luque T., Hjelmqvist L., Gonzalez-Duarte R.,
RA Joernvall H.;
RT "Fundamental molecular differences between alcohol dehydrogenase classes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4980-4984(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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.
CC {ECO:0000269|PubMed:8197167}.
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:0000269|PubMed:8197167};
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:0000269|PubMed:8197167};
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:0000269|PubMed:8197167};
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:0000269|PubMed:8197167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + octan-1-ol = H(+) + NADH + octanal;
CC Xref=Rhea:RHEA:24620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16188,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.73;
CC Evidence={ECO:0000269|PubMed:8197167};
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR EMBL; U07799; AAA57187.1; -; Genomic_DNA.
DR EMBL; U07641; AAB02520.1; -; mRNA.
DR EMBL; AE014297; AAF54571.1; -; Genomic_DNA.
DR EMBL; AY089518; AAL90256.1; -; mRNA.
DR EMBL; AY089615; AAL90353.1; -; mRNA.
DR PIR; S51357; S51357.
DR RefSeq; NP_524310.1; NM_079586.4.
DR AlphaFoldDB; P46415; -.
DR SMR; P46415; -.
DR BioGRID; 66455; 4.
DR DIP; DIP-23839N; -.
DR IntAct; P46415; 1.
DR STRING; 7227.FBpp0081767; -.
DR iPTMnet; P46415; -.
DR PaxDb; P46415; -.
DR PRIDE; P46415; -.
DR DNASU; 41311; -.
DR EnsemblMetazoa; FBtr0082290; FBpp0081767; FBgn0011768.
DR GeneID; 41311; -.
DR KEGG; dme:Dmel_CG6598; -.
DR CTD; 41311; -.
DR FlyBase; FBgn0011768; Fdh.
DR VEuPathDB; VectorBase:FBgn0011768; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00940000164379; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P46415; -.
DR OMA; IHHYMGT; -.
DR OrthoDB; 664798at2759; -.
DR PhylomeDB; P46415; -.
DR Reactome; R-DME-2161541; Abacavir metabolism.
DR Reactome; R-DME-5365859; RA biosynthesis pathway.
DR Reactome; R-DME-71384; Ethanol oxidation.
DR SABIO-RK; P46415; -.
DR BioGRID-ORCS; 41311; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41311; -.
DR PRO; PR:P46415; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011768; Expressed in spermathecum and 29 other tissues.
DR Genevisible; P46415; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:FlyBase.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0018467; F:formaldehyde dehydrogenase activity; ISS:FlyBase.
DR GO; GO:0004552; F:octanol dehydrogenase activity; IDA:FlyBase.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IDA:FlyBase.
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:0080007; F:S-nitrosoglutathione reductase activity; IMP:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0006066; P:alcohol metabolic process; IC:FlyBase.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR GO; GO:0080164; P:regulation of nitric oxide metabolic process; IC:FlyBase.
DR GO; GO:2000169; P:regulation of peptidyl-cysteine S-nitrosylation; IMP:FlyBase.
DR GO; GO:0008542; P:visual learning; IMP:FlyBase.
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 Acetylation; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..379
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000160769"
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:8197167"
SQ SEQUENCE 379 AA; 40389 MW; 7F382E10BFACAAC1 CRC64;
MSATEGKVIT CKAAVAWEAK KPLVIEDIEV APPKAHEVRI KITATGVCHT DAFTLSGADP
EGLFPVVLGH EGAGIVESVG EGVTNFKAGD HVIALYIPQC NECKFCKSGK TNLCQKIRLT
QGAGVMPEGT SRLSCKGQQL FHFMGTSTFA EYTVVADISL TKINEKAPLE KVCLLGCGIS
TGYGAALNTA KVEAGSTCAV WGLGAVGLAV GLGCKKAGAG KIYGIDINPD KFELAKKFGF
TDFVNPKDVA DKGSIQNYLI DLTDGGFDYT FECIGNVNTM RSALEATHKG WGTSVVIGVA
GAGQEISTRP FQLVVGRVWK GSAFGGWRSV SDVPKLVEDY LKKDLLVDEF ITHELPLSQI
NEAFDLMHKG ESIRSIIKY
