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Database: UniProt
Entry: A0A1U7DDG5_9RHOB
LinkDB: A0A1U7DDG5_9RHOB
Original site: A0A1U7DDG5_9RHOB 
ID   A0A1U7DDG5_9RHOB        Unreviewed;       530 AA.
AC   A0A1U7DDG5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=Ga0080559_TMP15 {ECO:0000313|EMBL:APX26116.1};
OS   Salipiger profundus.
OG   Plasmid ptpro4 {ECO:0000313|Proteomes:UP000186559}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX26116.1, ECO:0000313|Proteomes:UP000186559};
RN   [1] {ECO:0000313|EMBL:APX26116.1, ECO:0000313|Proteomes:UP000186559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2016 {ECO:0000313|EMBL:APX26116.1,
RC   ECO:0000313|Proteomes:UP000186559};
RC   PLASMID=Plasmid ptpro4 {ECO:0000313|Proteomes:UP000186559};
RA   Tang K.;
RT   "Deep-sea bacteria in the southern Pacific.";
RL   Submitted (MAR-2016) 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}.
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DR   EMBL; CP014800; APX26116.1; -; Genomic_DNA.
DR   RefSeq; WP_076625776.1; NZ_FOLR01000024.1.
DR   AlphaFoldDB; A0A1U7DDG5; -.
DR   KEGG; tpro:Ga0080559_TMP15; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000186559; Plasmid ptpro4.
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.
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}; Plasmid {ECO:0000313|EMBL:APX26116.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186559}.
FT   DOMAIN          11..387
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          410..516
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   530 AA;  59111 MW;  741BFECC282C447B CRC64;
     MGTEDQTDIV DIFVIGGGIN GCGIARDAAG RGLSVTLAEM SDLASATSSA STKLFHGGLR
     YLEFFEFRLV REALIEREVL LQAMPHISWP MRFVLPYHRD MRFESATPTS RLLSTVMPWM
     KGRRPAWLIR LGLFLYDTLG GRKILPGTAT LSLKGTPEGV PLQDHFETAY EYSDCWIEDS
     RLVVLNARDA EARGAQILTR AKVLSADRSA DHWTIEVEDV VTGQRTRHRS RMVVNAGGPW
     VGELLQGTIR LNSREGVRLV RGSHIVTGRL TDHDKCYFFQ GKDGRIIFAI PYETDFTLIG
     TTDQDHADPD QRPVCTPEEQ QYLIDFANGY FRQQMTRDDI VWTYSGVRPL YDDGASSATA
     ATRDYTLKVD TAGAPVLNVF GGKITTYRRL AESALEKISA ALGRDTAPWT AGVALPGGDF
     DVWDVERLIA DLIAGYPFLD DRWARRLIRA YGTEARKILG DAATAANMGR DFGATLTEAE
     VRWLMAQEYA RTAEDVVWRR NKLGLRLSNE EVQALDSWME DQRAAVAAAE
//
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