ID ADHX_MAIZE Reviewed; 381 AA. AC P93629; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 02-SEP-2026, entry version 152. DE RecName: Full=Alcohol dehydrogenase class-3; DE EC=1.1.1.1 {ECO:0000250|UniProtKB:Q96533}; 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:Q96533}; GN Name=FDH; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=cv. Black Mexican Sweet; RX PubMed=9290637; DOI=10.1023/a:1005872222490; RA Fliegmann J., Sandermann H. Jr.; RT "Maize glutathione-dependent formaldehyde dehydrogenase cDNA: a novel plant RT gene of detoxification."; RL Plant Mol. Biol. 34:843-854(1997). CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary alcohol + NAD(+) = an aldehyde + NADH + H(+); 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:Q96533}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a secondary alcohol + NAD(+) = a ketone + NADH + H(+); 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:Q96533}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-(hydroxymethyl)glutathione + NADP(+) = S-formylglutathione + CC NADPH + H(+); 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:Q96533}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-(hydroxymethyl)glutathione + NAD(+) = S-formylglutathione + CC NADH + H(+); 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:Q96533}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:Q96533}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q96533}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96533}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06525}. CC -!- TISSUE SPECIFICITY: Expressed at low levels in the leaves. CC {ECO:0000269|PubMed:9290637}. CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase CC family. Class-III subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y11029; CAA71913.1; -; mRNA. DR PIR; T03289; T03289. DR RefSeq; NP_001105485.2; NM_001112015.2. DR AlphaFoldDB; P93629; -. DR SMR; P93629; -. DR FunCoup; P93629; 3418. DR STRING; 4577.P93629; -. DR PaxDb; 4577-P93629; -. DR GeneID; 542459; -. DR KEGG; zma:542459; -. DR eggNOG; KOG0022; Eukaryota. DR InParanoid; P93629; -. DR OrthoDB; 417550at2759; -. DR Proteomes; UP000007305; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central. DR CDD; cd08300; alcohol_DH_class_III; 1. DR FunFam; 3.40.50.720:FF:000003; S-(hydroxymethyl)glutathione dehydrogenase; 1. DR FunFam; 3.90.180.10:FF:000001; S-(hydroxymethyl)glutathione dehydrogenase; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR013149; ADH-like_C. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR014183; ADH_3. DR InterPro; IPR002328; ADH_Zn_CS. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02818; adh_III_F_hyde; 1. DR PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1. DR PANTHER; PTHR43880:SF58; ALCOHOL DEHYDROGENASE CLASS-3; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF00107; ADH_zinc_N; 1. DR SUPFAM; SSF50129; GroES-like; 2. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00059; ADH_ZINC; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1..381 FT /note="Alcohol dehydrogenase class-3" FT /id="PRO_0000160772" FT BINDING 49 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 50 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 51 FT /ligand="an alcohol" FT /ligand_id="ChEBI:CHEBI:30879" FT /evidence="ECO:0000250|UniProtKB:P06525" FT BINDING 71 FT /ligand="an alcohol" FT /ligand_id="ChEBI:CHEBI:30879" FT /evidence="ECO:0000250|UniProtKB:P00327" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 115 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 204..209 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 228 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 233 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 274 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 297..299 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 322..324 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" FT BINDING 374 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q96533" SQ SEQUENCE 381 AA; 40772 MW; EABC4BEEDF76B65A CRC64; MASPTQGQVI TCKAAVAYEP NKPLVIEDVQ VAPPQAGEVR VKILFTALCH TDHYTWSGKD PEGLFPCILG HEAAGIVESV GEGVTDVQPG DHVIPCYQAE CKECKFCKSG KTNLCGKVRS ATGVGVMMND MKSRFSVNGK PIYHFMGTST FSQYTVVHDV SVAKINPQAP LDKVCLLGCG VPTGLGAVWN TAKVESGSVV AVFGLGTVGL AVAEGAKAAG ASRVIGIDID NKKFDVAKNF GVTEFVNPKE HDKPIQQVLV DLTDGGVDYS FECIGNVSIM RAALECSDKG WGTSVIVGVA ASGQEISTRP FQLVTGRVWK GTAFGGFKSR TQVPWLVDKY MKKEIKVDEY ITHNMNLADI NDAFHLLHEG GCLRCVLAMQ I //