ID A0A2C9VLI6_MANES Unreviewed; 441 AA.
AC A0A2C9VLI6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-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 ORFNames=MANES_07G142700 {ECO:0000313|EMBL:OAY46423.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY46423.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY46423.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY46423.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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|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; CM004393; OAY46423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9VLI6; -.
DR STRING; 3983.A0A2C9VLI6; -.
DR EnsemblPlants; OAY46423; OAY46423; MANES_07G142700.
DR Gramene; OAY46423; OAY46423; MANES_07G142700.
DR OMA; KYHVKMP; -.
DR OrthoDB; 3675564at2759; -.
DR Proteomes; UP000091857; Chromosome lg7.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857}.
FT DOMAIN 110..269
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 289..429
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT REGION 47..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 47502 MW; A686424C9D225E49 CRC64;
MALKIEDNSI LTMTMALFEA PPSFNCNYPL FASSRNTSTV VISCSASSLP PPSSPKIPEG
GTTNPNSLNT APDRSRDRRK VVRLAWEKLV RWSRSWRSKN RTDVLQQTNK VVVLGGGSFG
TAMAAHVANR KADLEVHMLL RDPLVCQSIN DDHCNCKYFP EYKLPDNVIA TTDPKTALIG
ADYCLHAVPV QFSSSFLEGI SEFVDPGLPF ISLSKGLELN TLRMMSQIIP QALKNPRQPF
VALSGPSFAL ELMNKLPTAM VVASKDKKLA NATQQLLASS HLRISTSSDV TGVEIAGALK
NVLAIAAGIV EGMHLGNNSM AALVAQGCSE IRWLAMKMGA KPATITGLSG TGDIMLTCFV
NLSRNKTVGV RLGSGEQLDD ILNSMNQVAE GVSTAGAVIA LAQKYKVKMP VLTAVARIID
NELTPKKAVL ELMRLPQVEE V
//
