ID Q89SG4_BRADU Unreviewed; 516 AA.
AC Q89SG4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
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:BAC47701.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC47701.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC47701.1; -; Genomic_DNA.
DR RefSeq; NP_769076.1; NC_004463.1.
DR RefSeq; WP_011085223.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89SG4; -.
DR STRING; 224911.AAV28_09090; -.
DR EnsemblBacteria; BAC47701; BAC47701; BAC47701.
DR GeneID; 64022177; -.
DR KEGG; bja:blr2436; -.
DR PATRIC; fig|224911.44.peg.2001; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_0_5; -.
DR InParanoid; Q89SG4; -.
DR OrthoDB; 9766796at2; -.
DR PhylomeDB; Q89SG4; -.
DR Proteomes; UP000002526; 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; IBA:GO_Central.
DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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:UP000002526}.
FT DOMAIN 9..366
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 390..494
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 516 AA; 57101 MW; 2F84683A453B2140 CRC64;
MRLLERIFDL AIIGGGVNGC GIARDAVGRG NTVFLCEMND LASGTSSWST KLVHGGLRYL
EYYEFRLVRE ALIEREILWG IAPHIIRPLR FVLPHHAGLR PAWLLRLGLF LYDHIGGRHL
LPATRSVDLG RDEVGRPLIP NRYSRAFEYS DCFVDDARLV VLNARDAADK GAEIRTRTRA
TEIRQADGVW TVSMVNTLTG ARSQVQARAL VNAGGPWVED VLGRGAGVNA KAKVRLVQGS
HIVVKKLYDH DRAYMFQNAD GRIIFVIPYQ DDFTLIGTTD RDYDGDPAKV KATPEEIQYL
CAAASEYLAK PVTSEDVVWT YSGVRPLYDD GASEAKAATR DYVFELDTPG GSPLLSIYGG
KITTYRRLAE EALERLSPYL RSAKAREGWT GKWPLPGGDM DVSDIDGLIA ELQRGYPFLG
HAHARRLARA YGTRAIKLLG DAKSAADLGQ AFGATLTERE VRYLMANEWA VTAEDIVWRR
SKLGLRLSAD EVAALDDWIR TNAVLQSPLL EAGGRS
//