ID A0A1D2LG46_BROTH Unreviewed; 550 AA.
AC A0A1D2LG46;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=CNY62_07260 {ECO:0000313|EMBL:ATF26205.1};
OS Brochothrix thermosphacta (Microbacterium thermosphactum).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF26205.1, ECO:0000313|Proteomes:UP000243591};
RN [1] {ECO:0000313|EMBL:ATF26205.1, ECO:0000313|Proteomes:UP000243591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BI {ECO:0000313|EMBL:ATF26205.1,
RC ECO:0000313|Proteomes:UP000243591};
RA Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT Brochothrix thermosphacta Isolated from Ground Chicken.";
RL Submitted (SEP-2017) 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|ARBA:ARBA00000153,
CC 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 -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00004977}.
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; CP023483; ATF26205.1; -; Genomic_DNA.
DR RefSeq; WP_069125967.1; NZ_RSDU01000009.1.
DR AlphaFoldDB; A0A1D2LG46; -.
DR STRING; 2756.BFR44_10210; -.
DR KEGG; bths:CNY62_07260; -.
DR OrthoDB; 9766796at2; -.
DR UniPathway; UPA00618; UER00674.
DR Proteomes; UP000243591; 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:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217};
KW Reference proteome {ECO:0000313|Proteomes:UP000243591}.
FT DOMAIN 23..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..528
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 550 AA; 61388 MW; 9B3A361965430B43 CRC64;
MATTFSGLDR KNKLEQLTTE EFDILVIGGG ITGAGIALDG ATRGLKVAVV EMQDFAGGTS
SRSTKLVHGG LRYLKQFQIG VVAEVGRERA IVYENGPHVT TPEWMLLPFH KGGTFGSFST
SIGLKVYDFL AQVKKGERRK MLSPTETLKK EPLVKNKNLK GGGYYVEYRT DDARLTIEVM
KAAIAKGALA INYVKSNNFI YDDNRQIIGA DIVDVQTGEA YKVKAKQVVN AAGPWVDEVR
GKDYAKNNKQ LRLTKGVHIV FDQSVFPLRQ AVYFDTPDKR MVFAIPRDGK TYVGTTDTVY
EADKLHPKVN KADRDYIIEA IHYMFPKVNI TKDDVESSWS GVRPLIFEKG KDPSEISRKD
EIWEGESGLL TIAGGKLTGY RKMAENIVDV AVKRMPGHGF SEKTQTEHLP ISGGDFGGSK
NYDSFVAKKA REAVNFNLTE EEGHFLASKY GTNVDALYAY AKASQEADID PIVDAQLMYA
IENESVVRPV DFFIRRTGAV FFNVKWAQKW EAPVIAKMAR LFNWTDAQIQ EYTTDLYIEI
KDSIKPVDED
//
