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NAD-dependent glycerol dehydrogenase (EC 1.1.1.6) (Dha-forming NAD-dependent glycerol dehydrogenase)

 GOLD_LISIN              Reviewed;         254 AA.
Q92EU6;
12-APR-2017, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 100.
RecName: Full=NAD-dependent glycerol dehydrogenase {ECO:0000303|PubMed:22773791};
EC=1.1.1.6 {ECO:0000269|PubMed:22773791};
AltName: Full=Dha-forming NAD-dependent glycerol dehydrogenase {ECO:0000303|PubMed:22773791};
Name=golD {ECO:0000303|PubMed:22773791};
OrderedLocusNames=lin0362 {ECO:0000312|EMBL:CAC95595.1};
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
NCBI_TaxID=272626;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-680 / CLIP 11262;
PubMed=11679669; DOI=10.1126/science.1063447;
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(2001).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, ACTIVITY
REGULATION, INDUCTION, AND SUBSTRATE SPECIFICITY.
STRAIN=ATCC BAA-680 / CLIP 11262;
PubMed=22773791; DOI=10.1128/JB.00801-12;
Monniot C., Zebre A.C., Ake F.M., Deutscher J., Milohanic E.;
"Novel listerial glycerol dehydrogenase- and phosphoenolpyruvate-
dependent dihydroxyacetone kinase system connected to the pentose
phosphate pathway.";
J. Bacteriol. 194:4972-4982(2012).
-!- FUNCTION: Involved in the glycerol metabolism. Catalyzes the NAD-
dependent oxidation of glycerol to dihydroxyacetone (glycerone).
GolD specifically uses NAD. {ECO:0000269|PubMed:22773791}.
-!- CATALYTIC ACTIVITY: Glycerol + NAD(+) = glycerone + NADH.
{ECO:0000269|PubMed:22773791}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:22773791};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:22773791};
-!- ACTIVITY REGULATION: Inhibited by Zn(2+).
{ECO:0000269|PubMed:22773791}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22773791}.
-!- INDUCTION: Repressed by GolR. {ECO:0000269|PubMed:22773791}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; AL596164; CAC95595.1; -; Genomic_DNA.
PIR; AC1478; AC1478.
RefSeq; WP_003765224.1; NC_003212.1.
ProteinModelPortal; Q92EU6; -.
SMR; Q92EU6; -.
STRING; 272626.lin0362; -.
EnsemblBacteria; CAC95595; CAC95595; CAC95595.
KEGG; lin:lin0362; -.
eggNOG; ENOG4105CHR; Bacteria.
eggNOG; ENOG410XNW1; LUCA.
KO; K22251; -.
OMA; TPSFRLD; -.
OrthoDB; POG091H012M; -.
Proteomes; UP000002513; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0019563; P:glycerol catabolic process; IDA:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Glycerol metabolism; Magnesium;
Manganese; NAD; Oxidoreductase.
CHAIN 1 254 NAD-dependent glycerol dehydrogenase.
/FTId=PRO_0000439493.
NP_BIND 18 47 NAD(P). {ECO:0000250|UniProtKB:Q7Z4W1}.
ACT_SITE 160 160 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 164 164 NAD(P). {ECO:0000250|UniProtKB:Q7Z4W1}.
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


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