GPD2_CANGA
ID GPD2_CANGA Reviewed; 422 AA.
AC Q6FWJ7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] 2;
DE EC=1.1.1.8;
GN Name=GPD2; OrderedLocusNames=CAGL0C05137g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC ChEBI:CHEBI:57945; EC=1.1.1.8;
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CR380949; CAG58303.1; -; Genomic_DNA.
DR RefSeq; XP_445397.1; XM_445397.1.
DR AlphaFoldDB; Q6FWJ7; -.
DR SMR; Q6FWJ7; -.
DR STRING; 5478.XP_445397.1; -.
DR EnsemblFungi; CAG58303; CAG58303; CAGL0C05137g.
DR GeneID; 2886789; -.
DR KEGG; cgr:CAGL0C05137g; -.
DR CGD; CAL0127442; GPD2.
DR VEuPathDB; FungiDB:CAGL0C05137g; -.
DR eggNOG; KOG2711; Eukaryota.
DR HOGENOM; CLU_033449_2_4_1; -.
DR InParanoid; Q6FWJ7; -.
DR OMA; ICYEGRS; -.
DR Proteomes; UP000002428; Chromosome C.
DR GO; GO:0005829; C:cytosol; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:EnsemblFungi.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:EnsemblFungi.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006168; G3P_DH_NAD-dep.
DR InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..422
FT /note="Glycerol-3-phosphate dehydrogenase [NAD(+)] 2"
FT /id="PRO_0000138087"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 69..74
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 47005 MW; 4BDF81C8757F3EB9 CRC64;
MFVRLARIPR ITRHYRLGLF STQPKPKPNE YLYYRNKHKS KMEAPIKRSS SAVSLVELER
EPFKVTVIGS GNWGTTIAKV VAENTKANPQ VFQERVDMWV FDENIDGTML TEIINTKHQN
VKYLPNIDLP ENLVANPDLL KSVEGADILV FNIPHQFLPK IVDQLRGHVE PHVRAISCLK
GFEVGKKGVQ LLSTYITEEL GIECGALSGA NLAPEVAKEH WSETTVAYHI PKDYQGDGMD
VDHKVLKLLF HRPYFHVSVI DDVAGISIAG ALKNVVALGC GFVEGLGWGN NAAAAIQRVG
LGEIIKFGQM FFPESRVETY YQESAGVADL ITTCSGGRNV RVATHMAKTG KSAEDSEKEL
LNGQSAQGVI TCKEVHEWLS TCEMIEEFPL FEAVYKIVYE DVPMHKLPEM IEELDDIVVA
GQ
