ID B4F4M2_DEBHN Unreviewed; 355 AA.
AC B4F4M2;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 13-SEP-2023, entry version 59.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
DE Flags: Fragment;
GN Name=gpd1 {ECO:0000313|EMBL:CAQ53147.1};
OS Debaryomyces hansenii var. hansenii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=58641 {ECO:0000313|EMBL:CAQ53147.1};
RN [1] {ECO:0000313|EMBL:CAQ53147.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Kam473 {ECO:0000313|EMBL:CAQ53147.1};
RA Nguyen H.V., Gaillardin C., Neuveglise C.;
RT "Differentiation of Debaryomyces hansenii and Candida famata by rRNA gene
RT intergenic spacer fingerprinting and reassessment of phylogenetic
RT relationships among D. hansenii, C. famata, D. fabryi, C. flareri
RT (=D.subglobosus) and D. prosopidis: description of D. vietnamensis sp. nov.
RT closely related to D. nepalensis.";
RL FEMS Yeast Res. 9:641-662(2009).
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; AM992123; CAQ53147.1; -; Genomic_DNA.
DR AlphaFoldDB; B4F4M2; -.
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}.
FT DOMAIN 6..170
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 203..354
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 214
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 10..15
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 285..286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAQ53147.1"
FT NON_TER 355
FT /evidence="ECO:0000313|EMBL:CAQ53147.1"
SQ SEQUENCE 355 AA; 39212 MW; 2BE82BF6657CB1FC CRC64;
EKPFRVAIIG SGNWGTAVAK IVSENTAEKP QVFEKQVNMW VFEEEVDGQK LTEIINTKHE
NVKYLPEVKL PENLVANPDV VDTVKDADLL IFNIPHQFLP RVCKQLVGHV KPSARAISCL
KGLEVGPEGC KLLSQSINDT LGVHCGVLSG ANIANEVARE RWSETTIAYN IPDDFRGKGK
DIDEYVLKQL FHRTYFHVRV INDIIGASFA GALKNVVACA VGFVIGAGWG DNAKAAIMRI
GIREIIHFAS YYQKFGVKGP APESTTFTEE SAGVADLITT CSGGRNVKVA RYMIENNVDA
WEAEKIVLKG QSSQGILTAK EVHELLTNYN LADEFPLFEA TYRIIYENAD VNEFP
//
