ID A0A1E4SYI4_9ASCO Unreviewed; 386 AA.
AC A0A1E4SYI4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN ORFNames=CANARDRAFT_29095 {ECO:0000313|EMBL:ODV84566.1};
OS [Candida] arabinofermentans NRRL YB-2248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX NCBI_TaxID=983967 {ECO:0000313|EMBL:ODV84566.1, ECO:0000313|Proteomes:UP000094801};
RN [1] {ECO:0000313|Proteomes:UP000094801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-2248 {ECO:0000313|Proteomes:UP000094801};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001662,
CC ECO:0000256|RuleBase:RU361243};
CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC ECO:0000256|RuleBase:RU000437}.
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DR EMBL; KV453856; ODV84566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4SYI4; -.
DR STRING; 983967.A0A1E4SYI4; -.
DR OrthoDB; 3675564at2759; -.
DR Proteomes; UP000094801; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Reference proteome {ECO:0000313|Proteomes:UP000094801}.
FT DOMAIN 34..199
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 232..377
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 39..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 308..309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 308
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 386 AA; 42530 MW; 6995DD2D46393102 CRC64;
MSASERLQNI TSALSPPSNC STVLPEDIPQ HPFKITVVGS GNWGSTIAKV VAENAIERPQ
EFEKIVKMWV FEELIDGEKL TEIINTKHEN VKYLPDIKLP SNIVAVPDVA EACKDADLII
FNIPHQFLPR VLSQLKGKLL PTARAISCLK GLEVTPEGCK LLSTYITEEL GIECGALSGA
NLAPEVALCK WSETTVAYKI PHDFRGKGKD IDEIVLKHVF HRPYFHVRVI HDVAGVSIAG
ALKNIIAMAA GFVEGLGWGD NAKSAVMRIG LVELIRFAKT FFEDCHTNTF THESAGVADL
ITTCAGGRNV RVGKYMAQHK VSAQEAEKVL LNGMSCQGLY TTKEVYDFLS NMGKIDEFPL
FKSTYQIIYE GLPMEKLPEL LESLED
//
