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Database: UniProt
Entry: A0A0F5LQ14_9RHIZ
LinkDB: A0A0F5LQ14_9RHIZ
Original site: A0A0F5LQ14_9RHIZ 
ID   A0A0F5LQ14_9RHIZ        Unreviewed;       541 AA.
AC   A0A0F5LQ14;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 17.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=VW29_10855 {ECO:0000313|EMBL:KKB84460.1};
OS   Devosia limi DSM 17137.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Hyphomicrobiaceae; Devosia.
OX   NCBI_TaxID=1121477 {ECO:0000313|EMBL:KKB84460.1, ECO:0000313|Proteomes:UP000033608};
RN   [1] {ECO:0000313|EMBL:KKB84460.1, ECO:0000313|Proteomes:UP000033608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17137 {ECO:0000313|EMBL:KKB84460.1,
RC   ECO:0000313|Proteomes:UP000033608};
RA   Hassan Y.I., Lepp D., Zhou T.;
RL   Submitted (MAR-2015) 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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         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|RuleBase:RU361217};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU361217}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKB84460.1}.
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DR   EMBL; LAJF01000076; KKB84460.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKB84460; KKB84460; VW29_10855.
DR   PATRIC; fig|1121477.3.peg.3303; -.
DR   Proteomes; UP000033608; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000033608};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033608}.
FT   DOMAIN       21    352       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      419    510       DAO_C. {ECO:0000259|Pfam:PF16901}.
SQ   SEQUENCE   541 AA;  57371 MW;  7A149869C377502B CRC64;
     MAEPLANRAA LRDRMAGASV DVLVVGGGIT GAGVALDAAS RGFSVALVEQ GDFASGTSSR
     SSKMIHGGFR YLQTGDVALV RESLRERYAL QRNAAHLVTV MPFMIPLFLK GGVINPKLSR
     ALGGALWSYQ LAGAWRLGKR HRRLDHQAVS AHMSGLDMER IGAGYLFHDL RTDDARLTLA
     VLASAVGQGA AVLNYARCTG VSAFDRDGRT AHIAVGGENI EIRARVIVNA TGVWAQNFLD
     IAGIASDRQL APAKGTHLVV PRALTGNDIA VSLPTSDRRT ISVVNEGPFA YIGSTESTDP
     DDINQPSITQ SDVDYILSGV NRHLKRPIAP SDVTGGWAGF RPLISGGKSA RSSDLSRKHS
     ISVEAEGVVT VTGGKLTTYR EMAEGTVNAI CGILNRRVAC RTRDLKLHGF GPGASHLSDG
     QRLDKRYGTK AAAITQIVTM SPPLGHSVTP LGDTLLAEVV WGLQAEMAAS LADALLRRTR
     IALYDGRAVL ANAEQIGLIV GRGVGWSPSQ IALETEQLKS TLRHELGVLA HDLPTVVPCQ
     S
//
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