ADHX_DICDI
ID ADHX_DICDI Reviewed; 379 AA.
AC Q54TC2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Name=adh5; ORFNames=DDB_G0281865;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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:0000250|UniProtKB:P11766}.
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 -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000043; EAL66492.1; -; Genomic_DNA.
DR RefSeq; XP_640467.1; XM_635375.1.
DR AlphaFoldDB; Q54TC2; -.
DR SMR; Q54TC2; -.
DR STRING; 44689.DDB0238276; -.
DR PaxDb; Q54TC2; -.
DR PRIDE; Q54TC2; -.
DR EnsemblProtists; EAL66492; EAL66492; DDB_G0281865.
DR GeneID; 8623280; -.
DR KEGG; ddi:DDB_G0281865; -.
DR dictyBase; DDB_G0281865; adh5.
DR eggNOG; KOG0022; Eukaryota.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; Q54TC2; -.
DR OMA; IHHYMGT; -.
DR PhylomeDB; Q54TC2; -.
DR Reactome; R-DDI-2161541; Abacavir metabolism.
DR Reactome; R-DDI-5365859; RA biosynthesis pathway.
DR Reactome; R-DDI-71384; Ethanol oxidation.
DR PRO; PR:Q54TC2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; ISS:dictyBase.
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; ISS:dictyBase.
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 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..379
FT /note="Alcohol dehydrogenase class-3"
FT /id="PRO_0000345023"
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|UniProtKB:P11766"
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|UniProtKB:P11766"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
SQ SEQUENCE 379 AA; 40553 MW; 5E5B438509D3E3C8 CRC64;
MSTEGKVITC KAAVAWEAKK PLVIEDIEVQ PPQKGEVRIK ILYTGVCHTD SYTLSGSDPE
GIFPCILGHE GGGIVESIGE GVTSVKVGDH VIPLYIPECG TCKFCTSNKT NLCSKIRITQ
GKGQMPDGTT RFKCKGKEIF HFMGTSTFSQ YTVLPEISCC VVREDAPLDK VCLLGCGITT
GFGAAKITAK VEEGSTVAIF GLGAVGLSVA QGAVDCGAKR IIGIDNNETK FGPGKDFGCT
EFINPSKDLP EGKTIQQHLV DITDGGVDYS FECIGNVNVM RAALECCHKG WGVSTIVGVA
PAGAEISTRP FQLVTGRVWK GSAFGGVKSR SQLPSIIDKY MDKKLKVDEY VTFTYPLNEI
NTAFDVMHEG KSLRSVVNL
