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Database: UniProt
Entry: A0A1I5KM29_9SPHN
LinkDB: A0A1I5KM29_9SPHN
Original site: A0A1I5KM29_9SPHN 
ID   A0A1I5KM29_9SPHN        Unreviewed;       495 AA.
AC   A0A1I5KM29;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   ORFNames=SAMN04488060_0362 {ECO:0000313|EMBL:SFO86065.1};
OS   Erythrobacter nanhaisediminis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=604088 {ECO:0000313|EMBL:SFO86065.1, ECO:0000313|Proteomes:UP000199331};
RN   [1] {ECO:0000313|EMBL:SFO86065.1, ECO:0000313|Proteomes:UP000199331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7715 {ECO:0000313|EMBL:SFO86065.1,
RC   ECO:0000313|Proteomes:UP000199331};
RA   de Groot N.N.;
RL   Submitted (OCT-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,
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}.
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DR   EMBL; FOWZ01000001; SFO86065.1; -; Genomic_DNA.
DR   BioCyc; GCF_900115585:BM173_RS01800-MONOMER; -.
DR   Proteomes; UP000199331; 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:UP000199331};
KW   Flavoprotein {ECO:0000256|RuleBase:RU361217};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361217}.
FT   DOMAIN        6    359       DAO. {ECO:0000259|Pfam:PF01266}.
FT   DOMAIN      382    488       DAO_C. {ECO:0000259|Pfam:PF16901}.
SQ   SEQUENCE   495 AA;  55431 MW;  CA190D897D8AC117 CRC64;
     MSERFDLLVI GGGINGAGIA RDAAGRGLSV ALVEKDDLAS HTSSASTKLV HGGLRYLEHY
     EFRLVAESLR EREVLLANAP HIIWPLRFVL PHEPGMRPKW MLRAGLFLYD RLGGRKTLPG
     SHKVDLRDPP HRAILQDHLT SGFEYSDCWV EDSRLVVLTA MDAEERGAKV WMRTECIALE
     RKADHWVATL SDPDGERVVE AKAVVNAAGP FVDKVAKSAL GEGTPAHLRL VKGSHIIVPR
     AYSGDHAYIF QQADDRIVFA IPYERDFTLI GTTDLLYEGD LDHVEIAAEE REYLREAATR
     YLRSGITEED IVHTYSGVRP LYEDNAASNS TVTRDYVFEI DADGGAPILS VYGGKITTYR
     KLAEHALEKL ADHAEIPSQG WTAHAPLPGG DIEKGDFARF LWKASDRFSW VPPEMLLRLC
     RAYGTRIDRV LSDAHSLDEL GTHLGGDLYE AELRYLVDCE YARSAEDVLW RRSKLGLHLS
     DETQESVREW FSSRS
//
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