ID Q32AN8_SHIDS Unreviewed; 501 AA.
AC Q32AN8;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:ABB63617.1};
GN OrderedLocusNames=SDY_3649 {ECO:0000313|EMBL:ABB63617.1};
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267 {ECO:0000313|EMBL:ABB63617.1, ECO:0000313|Proteomes:UP000002716};
RN [1] {ECO:0000313|EMBL:ABB63617.1, ECO:0000313|Proteomes:UP000002716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197 {ECO:0000313|EMBL:ABB63617.1,
RC ECO:0000313|Proteomes:UP000002716};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
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DR EMBL; CP000034; ABB63617.1; -; Genomic_DNA.
DR RefSeq; WP_000448119.1; NC_007606.1.
DR RefSeq; YP_405108.1; NC_007606.1.
DR AlphaFoldDB; Q32AN8; -.
DR STRING; 300267.SDY_3649; -.
DR EnsemblBacteria; ABB63617; ABB63617; SDY_3649.
DR KEGG; sdy:SDY_3649; -.
DR PATRIC; fig|300267.13.peg.4331; -.
DR HOGENOM; CLU_015740_5_0_6; -.
DR OMA; QKWWEAP; -.
DR Proteomes; UP000002716; Chromosome.
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:UP000002716}.
FT DOMAIN 5..323
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 381..496
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 501 AA; 56749 MW; C439DE3C75093489 CRC64;
METKDLIVIG GGINGAGIAA DAAGRGLSVL MLEAQDLACA TSSASSKLIH GGLRYLEHYE
FRLVSEALAE REVLLKMAPH IAFPMRFRLP HRPHLRPAWM IRIGLFMYDH LGKRTSLPGS
TGLRFGANSV LKPEIKRGFE YSDCWVDDAR LVLANAQMVV RKGGEVLTRT RATSARRENG
LWIVEAEDID TGKKYSWQAR GLVNATGPWV KQFFDDGMHL PSPYGIRLIK GSHIVVPRVH
TQKQAYILQN EDKRIVFVIP WMDEFSIIGT TDVEYKGDPK AVKIEESEIN YLLKVYNAHF
KKQLSRDDIV WTYSGVRPLC DDESDSPQAI TRDYTLDIHD ENGKAPLLSV FGGKLTTYRK
LAEHALEKLT PYYQDIGPAW TKESVLPGGA IEGDRDDYAA RLRRRYPFLT ESLARHYART
YGSNSELLLG NAGAISDLGE DFGHEFYEAE LKYLVDHEWV RRADDALWRR TKQGMWLNAD
QQSRVSQWLV EYTQQKLSLA S
//