ID A5VZG5_PSEP1 Unreviewed; 512 AA. AC A5VZG5; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217}; DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217}; GN OrderedLocusNames=Pput_1114 {ECO:0000313|EMBL:ABQ77275.1}; OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ77275.1}; RN [1] {ECO:0000313|EMBL:ABQ77275.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F1 {ECO:0000313|EMBL:ABQ77275.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.; RT "Complete sequence of Pseudomonas putida F1."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; CC Evidence={ECO:0000256|RuleBase:RU361217}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU361217}; CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330, CC ECO:0000256|RuleBase:RU361217}. 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; CP000712; ABQ77275.1; -; Genomic_DNA. DR AlphaFoldDB; A5VZG5; -. DR KEGG; ppf:Pput_1114; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_5_0_6; -. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 6.10.250.1890; -; 1. DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR031656; DAO_C. DR InterPro; IPR038299; DAO_C_sf. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR000447; G3P_DH_FAD-dep. DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF16901; DAO_C; 1. DR PRINTS; PR01001; FADG3PDH. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00977; FAD_G3PDH_1; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU361217}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361217}. FT DOMAIN 16..369 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 391..496 FT /note="Alpha-glycerophosphate oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF16901" SQ SEQUENCE 512 AA; 56821 MW; CEDCBF4E4A25109F CRC64; MSQPVSSQPP TADCYDLVVI GGGINGVGIA ADAAGRGLKV FLCEKDDLAQ HTSSASSKLI HGGLRYLEHY EFRLVREALA EREVLLAKAP HIVKPMRFVL PHRPHLRPAW MIRAGLFLYD HLGKRKRLGA SRSLRFGPGY PLKPAITRGF EYADCAVDDA RLVVLNAMAA RELGAHIHTR TRCLRAERVE GLWQVELQHA DGSLQTIHAR ALVNAAGPWV ASFIKDDLKL DAPYGIRLIQ GSHIIVPRLY EGEHAYILQN EDQRIVFCIP YLDRFTLIGT TDREYSGDPA AVAITEQETH YLLKVVNEHF NHQLSQADIL HTYSGVRPLC NDESDNPSAV TRDYTLALSA EAGQAPLLSV FGGKLTTYRK LAESAMAELK PFFTQMRGPW TASAPLPGAE GMTTVQALID AVLARCGWLP VDLAKRWVLT YGSRVWRLLD GVHGPEDLGQ AIGAGLFTRE VDYLLEEEWA EQTADIIWRR TKLGLSLTAQ EQIALEAYLQ QARKVRTNSR AA //