ID   GOLD_LISIN              Reviewed;         254 AA.
AC   Q92EU6;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=NAD-dependent glycerol dehydrogenase {ECO:0000303|PubMed:22773791};
DE            EC=1.1.1.6 {ECO:0000269|PubMed:22773791};
DE   AltName: Full=Dha-forming NAD-dependent glycerol dehydrogenase {ECO:0000303|PubMed:22773791};
GN   Name=golD {ECO:0000303|PubMed:22773791};
GN   OrderedLocusNames=lin0362 {ECO:0000312|EMBL:CAC95595.1};
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, ACTIVITY
RP   REGULATION, INDUCTION, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=22773791; DOI=10.1128/jb.00801-12;
RA   Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
RT   "Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-dependent
RT   dihydroxyacetone kinase system connected to the pentose phosphate
RT   pathway.";
RL   J. Bacteriol. 194:4972-4982(2012).
CC   -!- FUNCTION: Involved in the glycerol metabolism. Catalyzes the NAD-
CC       dependent oxidation of glycerol to dihydroxyacetone (glycerone). GolD
CC       specifically uses NAD. {ECO:0000269|PubMed:22773791}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH;
CC         Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC         ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6;
CC         Evidence={ECO:0000269|PubMed:22773791};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:22773791};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:22773791};
CC   -!- ACTIVITY REGULATION: Inhibited by Zn(2+).
CC       {ECO:0000269|PubMed:22773791}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22773791}.
CC   -!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AL596164; CAC95595.1; -; Genomic_DNA.
DR   PIR; AC1478; AC1478.
DR   RefSeq; WP_003765224.1; NC_003212.1.
DR   AlphaFoldDB; Q92EU6; -.
DR   SMR; Q92EU6; -.
DR   STRING; 272626.lin0362; -.
DR   EnsemblBacteria; CAC95595; CAC95595; CAC95595.
DR   GeneID; 61169369; -.
DR   KEGG; lin:lin0362; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_1_1_9; -.
DR   OMA; DGPLDHY; -.
DR   OrthoDB; 1294334at2; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycerol metabolism; Magnesium; Manganese; NAD; Oxidoreductase.
FT   CHAIN           1..254
FT                   /note="NAD-dependent glycerol dehydrogenase"
FT                   /id="PRO_0000439493"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         18..47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT   BINDING         164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
SQ   SEQUENCE   254 AA;  27262 MW;  676A505A57A1CEF9 CRC64;
     MTFKGFDKDF NITDKVAVVT GAASGIGKAM AELFSEKGAY VVLLDIKEDV KDVAAQINPS
     RTLALQVDIT KKENIEKVVA EIKKVYPKID ILANSAGVAL LEKAEDLPEE YWDKTMELNL
     KGSFLMAQII GREMIATGGG KIVNMASQAS VIALDKHVAY CASKAAIVSM TQVLAMEWAP
     YNINVNAISP TVILTELGKK AWAGQVGEDM KKLIPAGRFG YPEEVAACAL FLVSDAASLI
     TGENLIIDGG YTIK