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Database: UniProt
Entry: A0A0K8P2V4_IDESA
LinkDB: A0A0K8P2V4_IDESA
Original site: A0A0K8P2V4_IDESA 
ID   A0A0K8P2V4_IDESA        Unreviewed;       518 AA.
AC   A0A0K8P2V4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=ISF6_2345 {ECO:0000313|EMBL:GAP36505.1};
OS   Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Piscinibacter.
OX   NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP36505.1, ECO:0000313|Proteomes:UP000037660};
RN   [1] {ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC   {ECO:0000313|Proteomes:UP000037660};
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "Discovery of a poly(ethylene terephthalate assimilation.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAP36505.1, ECO:0000313|Proteomes:UP000037660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC   {ECO:0000313|Proteomes:UP000037660};
RX   PubMed=26965627; DOI=10.1126/science.aad6359;
RA   Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA   Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT   "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL   Science 351:1196-1199(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAP36505.1}.
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DR   EMBL; BBYR01000036; GAP36505.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K8P2V4; -.
DR   STRING; 1547922.ISF6_2345; -.
DR   Proteomes; UP000037660; Unassembled WGS sequence.
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.
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:UP000037660}.
FT   DOMAIN          2..335
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          386..495
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   518 AA;  57255 MW;  5AF30B82E0B06221 CRC64;
     MLVVGGGING AGIARDLAGR GHRVLLCERD DLAAHTSSAS TKLIHGGLRY LEYFEFGLVR
     KALAERERLL RSAPHLIRPM RFVMPHDPGM RPAWMIRAGL FLYDHLASRE LLRASRGVNL
     REHVAGEALK PAYSRGFVYS DAWVDDARLV VANAQDAAER GATVRTRTAC IDARRGRERW
     TATLQGIDGR RQTVHARALV NAAGPWAGRF LADVAHQPAT QGLRLVKGSH LVVRRRFEHD
     HAYLFQTTDR RVVFAIPYED DCTLIGTTDV EQAGGPDTPR LDSAEAAYLC EQVSRYFLRP
     VTPADVVWSY AGLRPLLDDE AGDPSAVTRD YLLALDTTGP GPEAGREPAA PLLTVWGGKL
     TTFRRLAEEA AALLEGPLGR RGGPWTRDAS LPGGDLRRWI GTPQRPDTDF IRFVQAVALR
     HPELAPDTCR RLARAYGGRI ERLLADGLGG EVVPGLYEAE LRYLHQHEWA RSAEDVLWRR
     TKLGLHTGPA QQAALADWCL RHWGPAPRWG EGADVRAA
//
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