GLPD_SYNY3
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 03-AUG-2022, entry version 122.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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; 1148.1653437; -.
DR PaxDb; P74257; -.
DR EnsemblBacteria; BAA18351; BAA18351; BAA18351.
DR KEGG; syn:sll1085; -.
DR eggNOG; COG0578; Bacteria.
DR InParanoid; P74257; -.
DR OMA; CIVNAAG; -.
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:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
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; -; 1.
DR Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF51905; SSF51905; 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