ID   Q72RP5_LEPIC            Unreviewed;       550 AA.
AC   Q72RP5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
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:AAS70288.1};
GN   OrderedLocusNames=LIC_11699 {ECO:0000313|EMBL:AAS70288.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS70288.1, ECO:0000313|Proteomes:UP000007037};
RN   [1] {ECO:0000313|EMBL:AAS70288.1, ECO:0000313|Proteomes:UP000007037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS70288.1,
RC   ECO:0000313|Proteomes:UP000007037};
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA   Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA   De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA   Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA   Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS70288.1; -; Genomic_DNA.
DR   RefSeq; WP_001165152.1; NC_005823.1.
DR   AlphaFoldDB; Q72RP5; -.
DR   GeneID; 61141597; -.
DR   KEGG; lic:LIC_11699; -.
DR   HOGENOM; CLU_015740_4_1_12; -.
DR   Proteomes; UP000007037; Chromosome I.
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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
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; 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}.
FT   DOMAIN          36..391
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          414..530
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   550 AA;  61773 MW;  599345A80416E04E CRC64;
     MQICRGKETC KAGRVLKMEK QKRVDQISKL QKESFDILVI GGGSTGAGAA FDAAKRGYKT
     ALIERKDFAS GTSSRSTKLI HGGVRYLAQF HFKLIHEALT ERQRLLENAP HLVKPLKFVL
     PAYRFYERPY YGIGLTLYDI LASKGKLPSH KTVSKSETIS EFKAIKKEGL FGGITYYDAQ
     FNDARLNVLL ARSAQKEGAV VANRIELVSF IKKSGKIVGA NLKDLETAKT FPVYTKVIAN
     TTGIWVDHIR KLDDPRTFNV LSPSQGIHLV FSKERVPCTS AMIIPKTKDG RVVFIIPWED
     HVILGTTDTP IENPGEEPLP IGNEVQFLLD TGNEYLENPV TEKDILSVFV GIRPLISPEG
     NQDTKNISRE EVILVSNSGL VTMGGGKWST YRKMAEDLVD KLIQIGNLEV REKCSTKFYV
     YPGAADYSES LYQEIEKTYK IDTIFAKRLQ NYYGTEVFEV LGKKPKLLGK GIPYFEEEVL
     FAVNEEFALG VTDVLARRFR ILFVDLSLAQ KMVAPVAMVL SKQLKWKDKT KKAEESAAME
     LIESLRKSYR
//