ID A0A420DPQ4_9RHOB Unreviewed; 532 AA.
AC A0A420DPQ4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=C8N30_0745 {ECO:0000313|EMBL:RKE96192.1};
OS Sulfitobacter guttiformis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=74349 {ECO:0000313|EMBL:RKE96192.1, ECO:0000313|Proteomes:UP000284407};
RN [1] {ECO:0000313|EMBL:RKE96192.1, ECO:0000313|Proteomes:UP000284407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11458 {ECO:0000313|EMBL:RKE96192.1,
RC ECO:0000313|Proteomes:UP000284407};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (SEP-2018) 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 -!- 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:RKE96192.1}.
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DR EMBL; RAQK01000001; RKE96192.1; -; Genomic_DNA.
DR RefSeq; WP_025063141.1; NZ_RAQK01000001.1.
DR AlphaFoldDB; A0A420DPQ4; -.
DR STRING; 1443111.Z949_2735; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000284407; Unassembled WGS sequence.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000284407}.
FT DOMAIN 11..387
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 410..516
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 532 AA; 59461 MW; 1D8E4638100B878B CRC64;
MGQHENQDIV DLFVIGGGIN GCGIARDAVG RGLSVELAEM NDLASATSSA STKLFHGGLR
YLEYWEIRLV REALIERETL LRAMPHISWP MRFVLPYHKD MRFESDTPTS KVLNVLVPWL
KGRRPAWLIR FGLFMYDNLG GRKILKGTTS LNLKGTPEGA PLQDRLEKAY EYSDCWIEDS
RLVVLNARDA QARGAFINVR TKVISAAQVS GMWQITLEAQ GGERRIVTAR MIVNAGGPWV
EDVIRNTMRI NSTEGVRLVR GSHIITRKLY DHDKCYFFQG EDGRIIFTIP YETDFTLIGT
TDADHEDVHE KPVCTPEEQD YLLGFASKYL KKPVTRDDIV HTYSGVRPLY NDGATSATAA
TRDYVLKLDQ SAGAPVLSVF GGKITTYRKL AESALEKIAP FFAQTGPQWT AGVALPGGDF
PVDGVGPLTA ELKAKYPFLT ERWVNRLLKA YGTEAFDLLG DAKTEGDLGR NFGSNLTERE
VNWLVEREFA NTAEDIIWRR SKLGLRMASK EIDALDSWMV SSAANLPKHH PV
//
