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Database: UniProt
Entry: A0A218WBN5_PUNGR
LinkDB: A0A218WBN5_PUNGR
Original site: A0A218WBN5_PUNGR 
ID   A0A218WBN5_PUNGR        Unreviewed;       455 AA.
AC   A0A218WBN5;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, 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   Name=LOC116193969 {ECO:0000313|RefSeq:XP_031378568.1};
GN   ORFNames=CDL15_Pgr025717 {ECO:0000313|EMBL:OWM69868.1};
OS   Punica granatum (Pomegranate).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Punica.
OX   NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM69868.1, ECO:0000313|Proteomes:UP000197138};
RN   [1] {ECO:0000313|Proteomes:UP000197138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX   PubMed=28654223; DOI=10.1111/tpj.13625;
RA   Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA   Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT   "The pomegranate (Punica granatum L.) genome and the genomics of
RT   punicalagin biosynthesis.";
RL   Plant J. 91:1108-1128(2017).
RN   [2] {ECO:0000313|EMBL:OWM69868.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM69868.1};
RA   Xu C.;
RT   "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_031378568.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_031378568.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|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; MTKT01004810; OWM69868.1; -; Genomic_DNA.
DR   RefSeq; XP_031378568.1; XM_031522708.1.
DR   Proteomes; UP000197138; Unassembled WGS sequence.
DR   Proteomes; UP000515151; Chromosome 2.
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   HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 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   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|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000437}.
FT   DOMAIN          124..283
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          303..443
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   REGION          60..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  48950 MW;  205E5410CDCC2399 CRC64;
     MAAVVEPAFF NITLTQSSSS LPSNPPLFLR FRRHKPPSRA LIAGTSCSCL ADTSHSQASS
     ADLQLPQGTA ASSSSASSSS DDNFVPDRTR DRRKVVRLAW EKLVRWSRSW RSKARTDVLE
     RTKKVVVLGG GSFGTAMASH IANKKTQLEV HMLIRDPLVC QSINENHRNC KYFPEHKLPD
     NVIASTDPKS ALSDADYCLH AVPVQFSSAF IEGIAEYVDP SLPFISLSKG LELNTLRMMS
     QIIPRSLRNP RQPFVALSGP SFALELMNKL PTAMVVASKD KKLANAAQQL LASSYLRIST
     SSDVTGVEIA GALKNVLAIA AGIVEGMNLG NNSMAALVAQ GCSEIRWLAT KMGAKPTTIT
     GLSGTGDIML TCFVNLSRNR TVGVRLGSGE KLDDILSSMN QVAEGVSTAG AVIALAQKYN
     VKMPVLTAVA RIVDNELTPK KAVSELMNLP QVEEV
//
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