ID   D5ARC2_RHOCB            Unreviewed;       521 AA.
AC   D5ARC2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
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:ADE86927.1};
GN   OrderedLocusNames=RCAP_rcc03203 {ECO:0000313|EMBL:ADE86927.1};
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE86927.1, ECO:0000313|Proteomes:UP000002361};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SB1003;
RA   Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA   Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA   Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA   Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT   "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADE86927.1, ECO:0000313|Proteomes:UP000002361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC   {ECO:0000313|Proteomes:UP000002361};
RX   PubMed=20418398; DOI=10.1128/JB.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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; CP001312; ADE86927.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5ARC2; -.
DR   STRING; 272942.RCAP_rcc03203; -.
DR   KEGG; rcp:RCAP_rcc03203; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   Proteomes; UP000002361; 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; 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:UP000002361}.
FT   DOMAIN          9..384
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          406..502
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   521 AA;  56880 MW;  F2D479433878A64E CRC64;
     MSDQPGVVDL FIIGGGVNGC GIARDAAGRG LSVTLAEQGD LAQGTSSAST KLFHGGLRYL
     EFFEFRLVRE ALEERETLLV AMPHISWPLR FVLPVHAGIR FDTTTPTSRL LNLMFPWMKG
     RRPAWLLRLG LFLYDSMGGR KILPGTRKLD LTRDKIGRAL KPGMGLAWEY SDCWVDDARL
     VVLNARDAQA RGANVLVGTR VTAAARQGDL WRIETEGPAG KAVHLARGLV NAAGPWVGQV
     LGLIEGPKPA AQVRLVRGSH IVTRRLHDDP RALFLQGSDG RIIFIIPYEQ DFSLIGTTEA
     AHEAAPEAAA CSAAERDYLL AFVSQYLAKP VTARDVVWSY AGVRPLYDDG ASSATAASRD
     YVLDLQAGGP VLLNVFGGKI TTYRRLAEAA LAKLAPHFPG LGPDWTARVP LPGGDFFQTG
     VKALIERLRV RYAFLGQAGA GRMVRAYGTE AFAILGEAKT RADLGRDFGA GLSEAEVIWL
     MDREWARRAE DVVWRRTKLG LRLSADQIAV LDRFMLERGA R
//