ID A0A135IBG8_9GAMM Unreviewed; 504 AA.
AC A0A135IBG8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:KXF82694.1};
GN ORFNames=ATN88_14505 {ECO:0000313|EMBL:KXF82694.1};
OS Enterovibrio coralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Enterovibrio.
OX NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF82694.1, ECO:0000313|Proteomes:UP000070529};
RN [1] {ECO:0000313|EMBL:KXF82694.1, ECO:0000313|Proteomes:UP000070529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF82694.1,
RC ECO:0000313|Proteomes:UP000070529};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (NOV-2015) 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:KXF82694.1}.
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DR EMBL; LNTY01000017; KXF82694.1; -; Genomic_DNA.
DR RefSeq; WP_067412541.1; NZ_LNTY01000017.1.
DR AlphaFoldDB; A0A135IBG8; -.
DR STRING; 294935.ATN88_14505; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000070529; 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:UP000070529}.
FT DOMAIN 7..360
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 383..493
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 504 AA; 56558 MW; E8E40E2F02AD35A4 CRC64;
MSDGVFDVLV VGGGINGAGI AADAAGRGLK VGLYEAADFA SATSSASSKL IHGGLRYLEH
YEFRLVSEAL AEREVLLRKA PYLAWPMRFR LPHRPHLRPA WMIRAGLFLY DHLSSRTTLP
GSKGIRFGES SVLKPEIKQG FEYSDCWVDD ARLVILNVMD AAERGAEVRN RCKVVSAERK
EGLWEIEVLD EVTQTRFTRK GKALVNAAGP WVKQFFDEST TETSPRNIRL IKGSHIVVPR
VHNESSSYIL QNEDGRIVFV LPYLDRFSLI GTTDVEYNGD PRNVGIEDKE IAYVLDVYNQ
HFKKPLTKDD VVWTYSGVRP LCDDESDSPQ AITRDYTLEL EASEGKAPIL SVFGGKLTTY
RKLAQAAVNQ LAPFFPDSTG EWTATQVLPG GEDISSFTEI EDALRQLHPW MEPFMVNRLA
TTYGSRVWVW LGDTSDKQDL GQQFGAGLSQ REIDYLTTAE YAQTAEDVLW RRTKLGLYLT
EEEREKVADY MAQKDAVALQ EEPV
//
