ID B7XPT9_ENTBH Unreviewed; 331 AA.
AC B7XPT9;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN ORFNames=EBI_24548 {ECO:0000313|EMBL:EED42039.1};
OS Enterocytozoon bieneusi (strain H348) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterocytozoon.
OX NCBI_TaxID=481877 {ECO:0000313|EMBL:EED42039.1, ECO:0000313|Proteomes:UP000001742};
RN [1] {ECO:0000313|EMBL:EED42039.1, ECO:0000313|Proteomes:UP000001742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348 {ECO:0000313|EMBL:EED42039.1,
RC ECO:0000313|Proteomes:UP000001742};
RX PubMed=18060071; DOI=10.1371/journal.pone.0001277;
RA Corradi N., Akiyoshi D.E., Morrison H.G., Feng X., Weiss L.M., Tzipori S.,
RA Keeling P.J.;
RT "Patterns of genome evolution among the microsporidian parasites
RT Encephalitozoon cuniculi, Antonospora locustae and Enterocytozoon
RT bieneusi.";
RL PLoS ONE 2:E1277-E1277(2007).
RN [2] {ECO:0000313|EMBL:EED42039.1, ECO:0000313|Proteomes:UP000001742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H348 {ECO:0000313|EMBL:EED42039.1,
RC ECO:0000313|Proteomes:UP000001742};
RX PubMed=19132089; DOI=10.1371/journal.ppat.1000261;
RA Akiyoshi D.E., Morrison H.G., Lei S., Feng X., Zhang Q., Corradi N.,
RA Mayanja H., Tumwine J.K., Keeling P.J., Weiss L.M., Tzipori S.;
RT "Genomic survey of the non-cultivatable opportunistic human pathogen,
RT Enterocytozoon bieneusi.";
RL PLoS Pathog. 5:E1000261-E1000261(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EED42039.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABGB01001135; EED42039.1; -; Genomic_DNA.
DR RefSeq; XP_002652017.1; XM_002651971.1.
DR AlphaFoldDB; B7XPT9; -.
DR STRING; 481877.B7XPT9; -.
DR VEuPathDB; MicrosporidiaDB:EBI_24548; -.
DR HOGENOM; CLU_033449_2_2_1; -.
DR InParanoid; B7XPT9; -.
DR OMA; EMITFAQ; -.
DR OrthoDB; 3675564at2759; -.
DR Proteomes; UP000001742; 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: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; IPR011128; G3P_DH_NAD-dep_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
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:UP000001742}.
FT DOMAIN 19..155
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 181..324
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 252..253
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ SEQUENCE 331 AA; 37171 MW; FD5DBD609400A229 CRC64;
MHSANLVATG IDACEFTSEV KVYVHETEVE CDGVMMKLSE AIMKKRQNPV FLPGIRIRDE
IVAITDTKRI SEWDVVIICI PCKYLHMLSD VKFKSDAILV SLTKGLVLHQ DTLLTPSMYI
HEISGKTCSS LQGANIASEV ARGVLSECVL SSSSSQDREI LCRLFVKSRF KVLNIEYDPC
IEVYGAVKNI IALGYGILEG LGDHVGENTK AFYFGRGCRE IQKFVEVLGY TGNHFFESCG
VGDVFVSCLH GRNAHAGKEI AMQFCIGKED YRCDFSTWRQ QHMQGVETVA VVYEYLAAKN
LSAKFDLITI IYQILYHNAD PQELYIYLEK N
//
