ID   Q2ISA2_RHOP2            Unreviewed;       513 AA.
AC   Q2ISA2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=RPB_4217 {ECO:0000313|EMBL:ABD08908.1};
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD08908.1, ECO:0000313|Proteomes:UP000008809};
RN   [1] {ECO:0000313|EMBL:ABD08908.1, ECO:0000313|Proteomes:UP000008809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2 {ECO:0000313|EMBL:ABD08908.1,
RC   ECO:0000313|Proteomes:UP000008809};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000250; ABD08908.1; -; Genomic_DNA.
DR   RefSeq; WP_011443092.1; NC_007778.1.
DR   AlphaFoldDB; Q2ISA2; -.
DR   STRING; 316058.RPB_4217; -.
DR   KEGG; rpb:RPB_4217; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000008809; 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..363
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          387..498
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   513 AA;  56250 MW;  9CF5F09A64542C38 CRC64;
     MDRVFDLAII GGGINGCGIA RDAAGRGNSV FLCEMNDLAS GTSSWSTKLI HGGLRYLEYF
     EFRLVREALI ERERLWQIAP HIIGPLRFVL PHHSGLRPAW RLRLGLFLYD YIGGRRLLPP
     TRSVDLAHDE VGKPLIPGRF TRGFEYSDCF VDDARLVVLT ARDAAERGAE IRTRTRAAQV
     RQSGGIWEVT LEDTQSGVRN TIRARALVNA AGPWVEAVLA SGAGVNAASK VRLVQGSHIV
     VPKLYDHDRA YIFQNADGRI VFAIPYQGDF TLIGTTDRDY DGDPSQVKAT PDEISYLCDA
     VSAYFAGPVK PADVVWTFSG VRPLYDDGAS EAKAATRDYV FELDTPGGAP LLSIYGGKIT
     TYRRLSEEAL EKLAPYLKGK TAKEGWTAHQ PLPGGDFPVD GAPALITELT RDYPFLSAAH
     AHRLVHAYGT RARDLLGAAR SMADLGCDFG ATLTEAEVRY LINREWACSA DDIVWRRSKL
     GLRLPPSALA AIDQWIAAFR ASEKPQQHAG GRA
//