(data stored in SCRATCH zone)

SWISSPROT: Q75CR7_ASHGO

ID   Q75CR7_ASHGO            Unreviewed;       381 AA.
AC   Q75CR7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
GN   ORFNames=AGOS_ACL148C {ECO:0000313|EMBL:AAS51080.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51080.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51080.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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:0000256|RuleBase:RU362016};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU362016};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000256|RuleBase:RU362016}.
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DR   EMBL; AE016816; AAS51080.1; -; Genomic_DNA.
DR   RefSeq; NP_983256.1; NM_208609.1.
DR   STRING; 33169.AAS51080; -.
DR   EnsemblFungi; AAS51080; AAS51080; AGOS_ACL148C.
DR   GeneID; 4619376; -.
DR   KEGG; ago:AGOS_ACL148C; -.
DR   HOGENOM; HOG000294674; -.
DR   InParanoid; Q75CR7; -.
DR   KO; K00121; -.
DR   OMA; ATHKGWG; -.
DR   Proteomes; UP000000591; Chromosome III.
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:0033833; F:hydroxymethylfurfural reductase (NADH) activity; IEA:EnsemblFungi.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
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; IEA:EnsemblFungi.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR   GO; GO:0033859; P:furaldehyde metabolic process; IEA:EnsemblFungi.
DR   CDD; cd08300; alcohol_DH_class_III; 1.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR013149; ADH_C.
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;
DR   PRODOM; Q75CR7.
DR   SWISS-2DPAGE; Q75CR7.
KW   Metal-binding {ECO:0000256|RuleBase:RU362016};
KW   NAD {ECO:0000256|RuleBase:RU362016};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          36..162
FT                   /note="ADH_N"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          207..330
FT                   /note="ADH_zinc_N"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   381 AA;  40432 MW;  4BE120B4D789E067 CRC64;
     MSETQGKPIQ CTAAVAYAAG EPLRIEKVTV DPPKAHEVRI KIVNSAICHT DAYTLSGSDP
     EGLFPCILGH EGSGIVESVG EGVTNVKPGD HVVPLYTAEC QQCKFCVSGK TNLCGAVRAT
     QGKGVMPDGT SRFRNGKGET LYHFMGCSTF SEYTVVADVS VVAVDQQAPL ETVCLLGCGV
     TTGYGAAVKT ADVQEGDTVA VFGAGTVGLS VVQGAKARNA SRIIVVDIND AKREWASKFG
     ATDFINPKTD LKEGETIVAR LIEMTDGGLD HTFDCTGNTK VMRDALEACH KGWGQSIIIG
     VAAAGQEIST RPFQLVTGRV WKGSAFGGIK GRSEMGGLVR DYLNGTLKVQ EFVTHKRPFE
     EINSGFEDLH HGDCLRTVLS L
//

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