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Database: UniProt
Entry: A0A0D7K7T3_9BURK
LinkDB: A0A0D7K7T3_9BURK
Original site: A0A0D7K7T3_9BURK 
ID   A0A0D7K7T3_9BURK        Unreviewed;       530 AA.
AC   A0A0D7K7T3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:KJA10032.1};
GN   ORFNames=RP29_13295 {ECO:0000313|EMBL:KJA10032.1};
OS   Acidovorax temperans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA10032.1, ECO:0000313|Proteomes:UP000032566};
RN   [1] {ECO:0000313|EMBL:KJA10032.1, ECO:0000313|Proteomes:UP000032566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY4 {ECO:0000313|EMBL:KJA10032.1,
RC   ECO:0000313|Proteomes:UP000032566};
RA   Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT   "Isolation of bacteria from lake water.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}.
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:KJA10032.1}.
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DR   EMBL; JXYQ01000042; KJA10032.1; -; Genomic_DNA.
DR   RefSeq; WP_044399249.1; NZ_JXYQ01000042.1.
DR   AlphaFoldDB; A0A0D7K7T3; -.
DR   STRING; 80878.RP29_13295; -.
DR   PATRIC; fig|80878.5.peg.2435; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000032566; Unassembled WGS sequence.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
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; PS00978; FAD_G3PDH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032566}.
FT   DOMAIN          26..388
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          435..513
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   530 AA;  56926 MW;  4A96A461DF5D8117 CRC64;
     MTNVSAPFST QRSDLLDRLA QPHVYDLAVI GGGATGLGVA LDAAARGFSV VLVDSHDFAK
     GTSSRATKLV HGGVRYLAQG NISLVREALH ERTTLLSNAP HLAQPLAFVM PSYRFWETPF
     YGIGLTMYDA LAGKAGLGST QFLGRERTLQ CLPTARQDGL KGGVKYWDGQ FDDARLALAL
     ARTAAARGAL LVNYCPAKKL VHEGGRVTGF ECEDAETGRS FTVRARCVVN ATGVWVDGLR
     QMDGEAIGKP VKPMVAPSQG VHIVVDREFL PSDHALMVPK TADGRVLFAV PWLGKVILGT
     TDSPRQDVVR EPLPFKEEVA FILNESARYL SRAPKQEDIR SIWVGLRPLV KPQDEDGGNT
     KSISREHTVL ASRSGLVTVT GGKWTTYRAM AEDVLQKCFD TGVLPPKAAG ITNQLPLVGS
     PAGAVQHSIS NAPGIHLYGA EAAAVASLPG SAKELGGGLT EAMVRFAARF EYARTVEDVL
     ARRSRLLFLD ARKAIDMAPA VAGILQEELG IDPQLPAFLA LAQQYLRPEM
//
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