ID A0A258H4U7_9MICO Unreviewed; 517 AA.
AC A0A258H4U7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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};
DE Flags: Fragment;
GN ORFNames=B7Y93_09260 {ECO:0000313|EMBL:OYX52040.1};
OS Micrococcales bacterium 32-70-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales.
OX NCBI_TaxID=1970540 {ECO:0000313|EMBL:OYX52040.1, ECO:0000313|Proteomes:UP000231631};
RN [1] {ECO:0000313|EMBL:OYX52040.1, ECO:0000313|Proteomes:UP000231631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-70-13 {ECO:0000313|EMBL:OYX52040.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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}.
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:OYX52040.1}.
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DR EMBL; NCEJ01000214; OYX52040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258H4U7; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000231631; Unassembled WGS sequence.
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:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
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; PF12697; Abhydrolase_6; 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; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00957; NAD_G3PDH; 1.
PE 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NAD {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}.
FT DOMAIN 3..74
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01210"
FT DOMAIN 95..224
FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07479"
FT DOMAIN 290..494
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OYX52040.1"
SQ SEQUENCE 517 AA; 54151 MW; C87549ECEDD30AEC CRC64;
SNLASIRDIL PPDVPVVSLM KGVERGTGLR MSEVIEQELR VDRDRIAAVS GPNLALEIAK
REPTAAVVAS ASHDTAVAVA TIASNDYFRS FVNTDVIGTE FGGVLKNLIA VAVGIADGVG
YGENTKASII TRGLVELSAF AVAFGARPET MIGLAGLGDL IATCESPLSR NNTAGRLLGQ
GYGFEQVIAQ MNQTAEGLAS VGPILELAAS RGVSMPIVAQ VAQRAAGRIG PCSSHGFRHL
VRSVAYDVSR TVRRGPPGRA HPLDRLGAVI TSLAGGRVLA EKHGATPPRV VALHGWGRDG
TDFATILTGL DAVSIHLPGF GPAPAPETVW GSEDYAELVA EAIAAFAPVV IVAHSFGGRV
AARLAAARPE LVAGLVLTGV PLVKLHAPAA PPLGYRIARW ANRRGLLSDA RMDALRDRRG
SSDYRAAQGV LRGIMVRVVN ETYDDELAAL AGSTVPMRFV WGEHDTQAPT DAGRVAAERA
GAPFRVVPGT GHLLEGDLEL AVREELLGLL DERTRTV
//
