ID G5R6U6_SALSE Unreviewed; 502 AA.
AC G5R6U6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=LTSESEN_5426 {ECO:0000313|EMBL:EHC81265.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC81265.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC81265.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC81265.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC81265.1}.
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DR EMBL; AFCU01001732; EHC81265.1; -; Genomic_DNA.
DR AlphaFoldDB; G5R6U6; -.
DR PATRIC; fig|913082.3.peg.4232; -.
DR BioCyc; SENT913082:G120J-1270-MONOMER; -.
DR Proteomes; UP000005065; 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}.
FT DOMAIN 5..323
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..476
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 502 AA; 56907 MW; 31B93B1F5A333078 CRC64;
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
TGVRFGADSV LKPEIVRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATAARRENG
LWIVEAEDID TGKKYVWQAR GLVNATGPWV KQFFDEGMHL PSPYGIRLIK GSHIVVPRVH
NQKQAYILQN EDKRIVFVIP WMEEFSIIGT TDVEYKGDPK AVKIEESEIN YLLKVYNAHF
QKQLGRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
LAEHAMEKLA SYYPGIGPAW TKTCVLPGGD IDGSREDYAA KLRRRYPFLT ESLARHYSRT
YGSNTEWILG EATSLLDLGE DFGHEFYEAE LKYLVDHEWV RRTEDAIWRR TKEGMWLTAE
QQSRITQWLA AYVEKHQLSL AS
//
