ID   GLPD_SYNY3              Reviewed;         553 AA.
AC   P74257;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase;
DE            EC=1.1.5.3;
GN   Name=glpD; OrderedLocusNames=sll1085;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18351.1; -; Genomic_DNA.
DR   PIR; S75892; S75892.
DR   AlphaFoldDB; P74257; -.
DR   SMR; P74257; -.
DR   IntAct; P74257; 2.
DR   STRING; 1148.gene:10499227; -.
DR   PaxDb; 1148-1653437; -.
DR   EnsemblBacteria; BAA18351; BAA18351; BAA18351.
DR   KEGG; syn:sll1085; -.
DR   eggNOG; COG0578; Bacteria.
DR   InParanoid; P74257; -.
DR   PhylomeDB; P74257; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; FAD; Flavoprotein; Glycerol metabolism; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..553
FT                   /note="Glycerol-3-phosphate dehydrogenase"
FT                   /id="PRO_0000126106"
FT   BINDING         13..41
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   553 AA;  61575 MW;  7AB17D9B9C03762D CRC64;
     MRNFPEIQNT AYDLIVIGGG INGVGTARDG ALRGLKTLLI EKDDFASGTS SWSTRLIHGG
     LRYLEYFEFN LVRESLRERE VLLHTAPHLV QPLQLTIPVY DWSSRAYWEI QAGMILYDIL
     SFDKTLPSHR MLSPQQFQQL FRAAEKKGLK GGAQYFDGQV EYAERLDLEV TLSAQKAGAA
     MLNYVAVKGL EKGENNLITA IHCQDQLSGE KFTVNSAQAI VINTTGPWVD EVCGLAHRGG
     EPVAIVQERK IGGTKGSHIV VDPFPGAPAS ALYVEAFVDK RPYFIIPWLG KYLIGTTDHR
     YDGSLDRVKA SDDEIDYLIA ETNRVMPAAQ LTRQDVRFTY SGVRPLPYTD GKKAGSITRN
     HILYDHSQDG VNNLISLIGG KLTTYRQVGE EMVDKVYGKL RRSAPPCPTL TQPLPGAEAY
     PLSLETAMDK YGNHLERHSI QHLFCLYGAR AGDILALVHG APELGERIIP SLPDIKAQVV
     FAVQAEMAHT LVDICRRRTA IAMVTNDYGF SALAGICQTL TDHCGWTQEQ CDKQIQKYHE
     YMEQNCIPDY CLH
//