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Database: UniProt
Entry: A0A1Y0N129_9FLAO
LinkDB: A0A1Y0N129_9FLAO
Original site: A0A1Y0N129_9FLAO 
ID   A0A1Y0N129_9FLAO        Unreviewed;       331 AA.
AC   A0A1Y0N129;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU000439};
DE            EC=1.1.1.94 {ECO:0000256|RuleBase:RU000439};
GN   ORFNames=BTO07_11765 {ECO:0000313|EMBL:ARV15771.1};
OS   Polaribacter sp. SA4-12.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV15771.1, ECO:0000313|Proteomes:UP000195470};
RN   [1] {ECO:0000313|EMBL:ARV15771.1, ECO:0000313|Proteomes:UP000195470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA4-12 {ECO:0000313|EMBL:ARV15771.1,
RC   ECO:0000313|Proteomes:UP000195470};
RA   Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.94;
CC         Evidence={ECO:0000256|RuleBase:RU000439};
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; CP019334; ARV15771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0N129; -.
DR   OrthoDB; 9812273at2; -.
DR   Proteomes; UP000195470; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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:SF1; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)] 2, CHLOROPLASTIC; 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   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000437};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195470}.
FT   DOMAIN          6..163
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          183..322
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-1"
FT   BINDING         87
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
FT   BINDING         258..259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-2"
FT   BINDING         258
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000114-3"
SQ   SEQUENCE   331 AA;  37380 MW;  EA415C64304EB6A5 CRC64;
     MNEQKKIAVF GGGSWATAIV KMLSENLETI GWYMRNEQAI EHIKENDHNP NYLRSADIFA
     RQLDLSSNIN YIVENYDVLI FAIPSAFLTS ELKKLETSLE NKIIFSAIKG IVPETGLIIG
     EHFNKEYNIP LENIGVITGP CHAEEVAMER LSYLTIACQD EEKAEFISNS LKSWYIKTKI
     SDDIIGTEYA AMLKNIYAVA AGMAHGLGYG DNFQAVLMSN AIREMKRFIK KIHKMKRNIN
     NSAYLGDLLV TGYSVFSRNR QFGNMVGKGY TVKSAQMEMS MIAEGYYATK SAFKMKEESG
     ANTPIIDTVY NILYDNKSPQ KEFKKLTDKL D
//
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