ID A0A9E0TA86_UNCPS Unreviewed; 329 AA. AC A0A9E0TA86; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 08-NOV-2023, entry version 4. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394}; DE EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394}; GN ORFNames=JSR53_14485 {ECO:0000313|EMBL:MBS0508579.1}; OS Pseudomonadota bacterium. OC Bacteria; Pseudomonadota. OX NCBI_TaxID=1977087 {ECO:0000313|EMBL:MBS0508579.1, ECO:0000313|Proteomes:UP000811483}; RN [1] {ECO:0000313|EMBL:MBS0508579.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS CTRL-42 {ECO:0000313|EMBL:MBS0508579.1}; RX PubMed=33819658; RA Wang Y., Zhao R., Liu L., Li B., Zhang T.; RT "Selective enrichment of comammox from activated sludge using RT antibiotics."; RL Water Res. 197:0-0(2021). RN [2] {ECO:0000313|EMBL:MBS0508579.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZAS CTRL-42 {ECO:0000313|EMBL:MBS0508579.1}; RA Wang Y., Cao Y., Meng X., Hu T., Wang S., Cao K.; RL Submitted (JAN-2021) 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=1.1.1.94; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00394}; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00394, ECO:0000256|RuleBase:RU000439}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. CC {ECO:0000256|HAMAP-Rule:MF_00394}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009, CC ECO:0000256|HAMAP-Rule:MF_00394, 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:MBS0508579.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAFEES010000383; MBS0508579.1; -; Genomic_DNA. DR Proteomes; UP000811483; 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-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0008654; P:phospholipid biosynthetic 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 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. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_00394}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_00394}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00394}; KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209, KW ECO:0000256|HAMAP-Rule:MF_00394}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP- KW Rule:MF_00394}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..329 FT /note="Glycerol-3-phosphate dehydrogenase [NAD(P)+]" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5038975764" FT DOMAIN 2..155 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 176..316 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 187 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 7..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 104 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 104 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 136 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 251..252 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 277 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" SQ SEQUENCE 329 AA; 33763 MW; 0168030B91E31153 CRC64; MKIVVLGAGA WGTALAVSAA HASAHAVTLW ARDAQQAATM QAARCNQRYL PGVAFPPALQ VVAGDARALA AGAELVIIAT PMAALRDMLQ LLAGCQAPIA WLCKGFEAGT GLMAHEVCAQ VAPQLASGVL SGPSFALEVA RAQPTALVAA SARERVREAL VAAFHGHMLR VYASDDIVGV EVGGAVKNVL AIATGLCDGL QLGLNARAAL ITRGLAEMTR LGLALGARPD TFMGLSGLGD LVLTATGDLS RNRRVGLLLA GGQTLQQAVA SLGHVAEGVY SARTVVQRAR AAGVEMPIAE CVVALLDGRL RAADAVALLM EREPTVERH //