ID A0A250XF89_9CHLO Unreviewed; 682 AA.
AC A0A250XF89;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN ORFNames=CEUSTIGMA_g9124.t1 {ECO:0000313|EMBL:GAX81696.1};
OS Chlamydomonas eustigma.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=1157962 {ECO:0000313|EMBL:GAX81696.1, ECO:0000313|Proteomes:UP000232323};
RN [1] {ECO:0000313|EMBL:GAX81696.1, ECO:0000313|Proteomes:UP000232323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2499 {ECO:0000313|EMBL:GAX81696.1,
RC ECO:0000313|Proteomes:UP000232323};
RA Hirooka S., Hirose Y., Kanesaki Y., Higuchi S., Fujiwara T., Onuma R.,
RA Era A., Ohbayashi R., Uzuka A., Nozaki H., Yoshikawa H., Miyagishima S.Y.;
RT "Acidophilic green algal genome provides insights into adaptation to an
RT acidic environment.";
RL Submitted (AUG-2017) 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}.
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:GAX81696.1}.
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DR EMBL; BEGY01000069; GAX81696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A250XF89; -.
DR STRING; 1157962.A0A250XF89; -.
DR OrthoDB; 313420at2759; -.
DR Proteomes; UP000232323; 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 CDD; cd04309; HAD_PSP_eu; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1.
DR Pfam; PF12710; HAD; 1.
DR Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR PRINTS; PR00077; GPDHDRGNASE.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56784; HAD-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|RuleBase:RU000437};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000437};
KW Reference proteome {ECO:0000313|Proteomes:UP000232323}.
FT DOMAIN 286..456
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 477..626
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
SQ SEQUENCE 682 AA; 75221 MW; FC8E0A7290614B8C CRC64;
MLSIRCGIQM KIAGSNAMKR NLYPGRGRSI VMNGLAGFNG NGTPQSNFRP SKQVLDMWQR
AEAVCFDIDC TITVNDSLDL LAEHMGVGEQ VAELTSKAMD GSMNLESSLE ERLKIINCKP
VDIKSFLEKH PPESRFAQGI QSLISSLQSR GVTIYLITGG FRELALPIAD KLNIPRENVF
ANRMLWQWDD ETLEPSRLVG FDMSEPTARN QGKPQAIAQI REKNSYNSVV MIGDGITDLE
AVQVSGGADL FIGFGGVEKR PKVQAEADWF VTDYADLEAA FLQSMQVAVI GSGSFAFAAA
RMVAQNAKES SASMFRDKVK IWVRPGSEFE GQSMIDIINE KHENPKYLPG IPLPENLEAF
SDLDQVIEGA DILVICTPHQ YIRGILKQIS GKVKSSTIAI SLVKGLRVRA DGPQLISQLV
RRSLGTDCSV LMGANIADEL AKEEFGEAVI GYDNIDNARI LKKLFQRPYF RVNLIPDAAG
AEMCGTLKNV VAIAAGLVEG LGYGANSKAA IMRQGLSEMM KFSIRLYPGI REETFLESCG
VADLVATCYG GRNRMVAMEY AKRWLVGQPE SFDALEAALL NGQKLQGVMT SEEVQEILAT
RGWERDFPLF TTINRIINYQ LDPSFVVKYE EGAQRPVLAK QLAANTYSWF PPPMPTEPIT
PVTQEPVPVP RRAPFDIFSM FK
//
