ID A0A066UTI7_9VIBR Unreviewed; 519 AA.
AC A0A066UTI7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:KDN29177.1};
GN ORFNames=VFDL14_18200 {ECO:0000313|EMBL:KDN29177.1};
OS Vibrio fortis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN29177.1, ECO:0000313|Proteomes:UP000027219};
RN [1] {ECO:0000313|EMBL:KDN29177.1, ECO:0000313|Proteomes:UP000027219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dalian14 {ECO:0000313|EMBL:KDN29177.1,
RC ECO:0000313|Proteomes:UP000027219};
RA Wang Y., Song L., Liu G., Ding J.;
RT "Vibrio fortis Dalian14 Genome Sequencing.";
RL Submitted (FEB-2014) 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:KDN29177.1}.
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DR EMBL; JFFR01000012; KDN29177.1; -; Genomic_DNA.
DR RefSeq; WP_032550594.1; NZ_JFFR01000012.1.
DR AlphaFoldDB; A0A066UTI7; -.
DR STRING; 212667.VFDL14_18200; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000027219; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 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 17..335
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 397..501
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 519 AA; 58256 MW; B25FE5B78E3208A8 CRC64;
MSAQQHNTNN GSSSTLDLIV IGGGINGAGI AADAAGRGLT VGLYEASDYA SATSSASSKL
IHGGLRYLEH YEFRLVSEAL AEREVLLRKA PHIAQPMRFR LPHRPFLRPA WMIRCGLFLY
DNLGKRTTLP ASKTVNLAQS GLLKPEMKVG FEYSDCWVDD ARMVLLNVLA AKENGAETRN
YCRVEAARRE GGVWVVTIRD VMTDQAFERK AKALVNAAGP WVKQFFDDGL EQESPRNIRL
IKGSHIVVPR IHDEPQAYIL QNKDNRIVFM IPYLDKFSII GTTDVEYKGD PREVAISDDE
VDYLIDIVNQ HFVQQLTTED VVWTYSGVRP LCDDESDSPQ AITRDYTLEL DAELDQAPLL
SVFGGKLTTY RKLGEAALKK LEPFLPNMGP AWTATDTLPG GNFSCSREQL ADMMNSKYPW
ASKGLLLRYI TQFGTQTWDL LAGATCEEDL GKKFSSEAHG VYQREIDYLI TQEMSQTSED
MLWRRTKLGL YMSEEEQQMV TNYLKTTLEQ KVVSFSQVS
//
