ID A0A1G7YS70_9VIBR Unreviewed; 519 AA.
AC A0A1G7YS70;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN04488136_10610 {ECO:0000313|EMBL:SDG99096.1};
OS Vibrio xiamenensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=861298 {ECO:0000313|EMBL:SDG99096.1, ECO:0000313|Proteomes:UP000198854};
RN [1] {ECO:0000313|EMBL:SDG99096.1, ECO:0000313|Proteomes:UP000198854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10228 {ECO:0000313|EMBL:SDG99096.1,
RC ECO:0000313|Proteomes:UP000198854};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNDD01000006; SDG99096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7YS70; -.
DR STRING; 861298.SAMN04488136_10610; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000198854; 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; 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:UP000198854}.
FT DOMAIN 18..336
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 393..492
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 519 AA; 58868 MW; 0117487C62DCC48F CRC64;
MNVNSSNYLH QDQDALLDLI VVGGGINGAG IAADAVGRGL SVGLYEAQDF ASATSSASSK
LIHGGLRYLE HYEFRLVSEA LAEREILLAK APHIAFPMRF RLPHQPYLRP AWMIRIGMFL
YDHLGKRTSL PASKKVALNA GVVTKPELKI GFEYSDCWVD DARLVILNIL QAQKLGAEVS
NYCEVESARR VGNHWQVNLI DHRSNTRFER RCKALVNATG PWVKSFIKDS IQTNSPYGIR
LIKGSHIIVN KLHDEPQAYI LQNEDKRIVF AIPYLDKFTM IGTTDLEYHG DPRQVEINAQ
ETQYLLDVIN NHFVKQLTQQ DIISSFSGVR PLCDDESDSP QAITRDYTLA LQSELDEAPL
LSVFGGKLTT YRKLAEAAME HLKPFFPAMK TSWTDGAPLP GGEEFDARAL EETYRHKMPE
VDTNTIKRWI HTYGTQMTAM LANVVTHKDL GREFAPGVYQ VEVDFLAKTE FALTARDILY
RRTKLNLLVD DEQLEHNIQR YLDEHYPPTQ DHHNERKYA
//
