ID A0A0G9HAJ9_9GAMM Unreviewed; 503 AA.
AC A0A0G9HAJ9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, 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=BJI69_10115 {ECO:0000313|EMBL:APG04215.1}, Y883_11325
GN {ECO:0000313|EMBL:KLD66835.1};
OS Luteibacter rhizovicinus DSM 16549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG04215.1, ECO:0000313|Proteomes:UP000182987};
RN [1] {ECO:0000313|EMBL:KLD66835.1, ECO:0000313|Proteomes:UP000035585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD66835.1,
RC ECO:0000313|Proteomes:UP000035585};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
RN [2] {ECO:0000313|EMBL:APG04215.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LJ96 {ECO:0000313|EMBL:APG04215.1};
RX PubMed=28123952;
RA Aamot H.U., Hofgaard I.S., Lysoe E.;
RT "Complete genome sequence of Luteibacter rhizovicinus strain LJ96T,
RT isolated from the rhizosphere of barley (Hordeum vulgare L.) in Denmark.";
RL Genom Data 11:104-105(2016).
RN [3] {ECO:0000313|Proteomes:UP000182987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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; CP017480; APG04215.1; -; Genomic_DNA.
DR EMBL; JPLB01000034; KLD66835.1; -; Genomic_DNA.
DR RefSeq; WP_046967876.1; NZ_JPLB01000034.1.
DR AlphaFoldDB; A0A0G9HAJ9; -.
DR STRING; 1440763.BJI69_10115; -.
DR KEGG; lrz:BJI69_10115; -.
DR PATRIC; fig|1440763.5.peg.2155; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000035585; Unassembled WGS sequence.
DR Proteomes; UP000182987; 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: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.
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 6..359
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 387..477
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 503 AA; 56567 MW; 0AD5886613A8D843 CRC64;
MVEQVDVLVV GGGVNGVGIA RDAVGRGLSV WLCERDDLAS HTSSAATKLI HGGLRYLEQF
EFALVGKALA EREVLLRAAP HIIWPLRFIL PHQPHLRPAW MIRIGLFLYD HLGRGRRTLP
GSRRVRFAKH VTGEPLRSEF HQGFVYSDAW VQDARLVVLN AMDAVHRGAK IETHTKCISA
RRDADGWTAE LEARDGSRHF VKARALVNAA GPWAASFLDD VVHLKHSHTL RLIKGSHIVV
PKIFDHRYAY IFQQPDRRIV FAIPYERDFT LIGTTDIEYK ADPSHPVIEA EETQYLCEAV
NRYFKKQLTP ADVVWSYSGV RPLLQDESGS ASEVTRDYLL DIDTDGAPLL NVFGGKLTTF
RKLSEEAVDK LAPLLGNDKP AWTADARPLP GGGERDIDAL TDDIRSSRPW LPETFAWRLT
HMYGTRARDL LGEANGLAAL GEHFGSDLYQ AEVDYLVRHE WATEAEDILW RRSKIGLRVG
PDDVRRLTEY LNRRVPQGAA THP
//