FADH_YEAST
ID FADH_YEAST Reviewed; 386 AA.
AC P32771; D6VRI3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000250|UniProtKB:P06525};
DE EC=1.1.1.284 {ECO:0000250|UniProtKB:P06525};
DE AltName: Full=Alcohol dehydrogenase SFA {ECO:0000303|PubMed:8483449};
DE EC=1.1.1.1 {ECO:0000269|PubMed:8483449};
DE AltName: Full=Glutathione-dependent formaldehyde dehydrogenase {ECO:0000303|PubMed:8483449};
DE Short=FALDH {ECO:0000305};
DE Short=FDH {ECO:0000305};
DE Short=FLD {ECO:0000305};
DE Short=GSH-FDH {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:8483449};
GN Name=SFA1; Synonyms=SFA; OrderedLocusNames=YDL168W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX PubMed=8483449; DOI=10.1007/bf00279438;
RA Wehner E.P., Rao E., Brendel M.;
RT "Molecular structure and genetic regulation of SFA, a gene responsible for
RT resistance to formaldehyde in Saccharomyces cerevisiae, and
RT characterization of its protein product.";
RL Mol. Gen. Genet. 237:351-358(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Oxidizes long-chain alcohols and, in the presence of
CC glutathione, is able to oxidize formaldehyde (PubMed:8483449). Is
CC responsible for yeast resistance to formaldehyde (PubMed:8483449).
CC {ECO:0000269|PubMed:8483449}.
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:P06525};
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:P06525};
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:8483449};
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:8483449};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P06525};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.34 mM for formaldehyde {ECO:0000269|PubMed:8483449};
CC KM=1.0 mM for methylglyoxal {ECO:0000269|PubMed:8483449};
CC KM=150 mM for butanol {ECO:0000269|PubMed:8483449};
CC KM=36 mM for pentanol {ECO:0000269|PubMed:8483449};
CC KM=19 mM for hexanol {ECO:0000269|PubMed:8483449};
CC KM=2.0 mM for octanol {ECO:0000269|PubMed:8483449};
CC KM=4.0 mM for 12-hydroxy-dodecanoate {ECO:0000269|PubMed:8483449};
CC KM=271 mM for allylalcohol {ECO:0000269|PubMed:8483449};
CC KM=0.09 mM for NAD(+) {ECO:0000269|PubMed:8483449};
CC KM=0.11 mM for glutathione {ECO:0000269|PubMed:8483449};
CC -!- INDUCTION: By formaldehyde, ethanol and methyl methanesulphonate.
CC {ECO:0000269|PubMed:8483449}.
CC -!- MISCELLANEOUS: Requires GSH for oxidation of formaldehyde or of
CC methylglyoxal, while oxidation of long-chain alcohols is independent of
CC GSH and enzyme activity improves with chain length.
CC {ECO:0000269|PubMed:8483449}.
CC -!- MISCELLANEOUS: Present with 8370 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-III subfamily. {ECO:0000305}.
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DR EMBL; X68020; CAA48161.1; -; Genomic_DNA.
DR EMBL; Z67750; CAA91578.1; -; Genomic_DNA.
DR EMBL; Z74216; CAA98742.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11693.1; -; Genomic_DNA.
DR PIR; S31140; S31140.
DR RefSeq; NP_010113.1; NM_001180228.1.
DR AlphaFoldDB; P32771; -.
DR SMR; P32771; -.
DR BioGRID; 31897; 163.
DR DIP; DIP-5366N; -.
DR IntAct; P32771; 1.
DR MINT; P32771; -.
DR STRING; 4932.YDL168W; -.
DR iPTMnet; P32771; -.
DR MaxQB; P32771; -.
DR PaxDb; P32771; -.
DR PRIDE; P32771; -.
DR EnsemblFungi; YDL168W_mRNA; YDL168W; YDL168W.
DR GeneID; 851386; -.
DR KEGG; sce:YDL168W; -.
DR SGD; S000002327; SFA1.
DR VEuPathDB; FungiDB:YDL168W; -.
DR eggNOG; KOG0022; Eukaryota.
DR GeneTree; ENSGT00970000196190; -.
DR HOGENOM; CLU_026673_14_0_1; -.
DR InParanoid; P32771; -.
DR OMA; IHHYMGT; -.
DR BioCyc; MetaCyc:YDL168W-MON; -.
DR BioCyc; YEAST:YDL168W-MON; -.
DR Reactome; R-SCE-2161541; Abacavir metabolism.
DR Reactome; R-SCE-5365859; RA biosynthesis pathway.
DR Reactome; R-SCE-71384; Ethanol oxidation.
DR PRO; PR:P32771; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32771; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:SGD.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR GO; GO:0033833; F:hydroxymethylfurfural reductase (NADH) activity; IMP:SGD.
DR GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IDA:SGD.
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:0000947; P:amino acid catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
DR GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR GO; GO:0046294; P:formaldehyde catabolic process; IDA:SGD.
DR GO; GO:0033859; P:furaldehyde metabolic process; IMP:SGD.
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 Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..386
FT /note="S-(hydroxymethyl)glutathione dehydrogenase"
FT /id="PRO_0000160785"
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="substrate"
FT /evidence="ECO:0000250|UniProtKB:P06525"
FT BINDING 71
FT /ligand="substrate"
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 300..302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
FT BINDING 325..327
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q96533"
SQ SEQUENCE 386 AA; 41042 MW; A495AFD7B47E4B11 CRC64;
MSAATVGKPI KCIAAVAYDA KKPLSVEEIT VDAPKAHEVR IKIEYTAVCH TDAYTLSGSD
PEGLFPCVLG HEGAGIVESV GDDVITVKPG DHVIALYTAE CGKCKFCTSG KTNLCGAVRA
TQGKGVMPDG TTRFHNAKGE DIYHFMGCST FSEYTVVADV SVVAIDPKAP LDAACLLGCG
VTTGFGAALK TANVQKGDTV AVFGCGTVGL SVIQGAKLRG ASKIIAIDIN NKKKQYCSQF
GATDFVNPKE DLAKDQTIVE KLIEMTDGGL DFTFDCTGNT KIMRDALEAC HKGWGQSIII
GVAAAGEEIS TRPFQLVTGR VWKGSAFGGI KGRSEMGGLI KDYQKGALKV EEFITHRRPF
KEINQAFEDL HNGDCLRTVL KSDEIK
