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Database: UniProt
Entry: U1YJ19_9BURK
LinkDB: U1YJ19_9BURK
Original site: U1YJ19_9BURK 
ID   U1YJ19_9BURK            Unreviewed;       518 AA.
AC   U1YJ19;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:ERI35083.1};
GN   ORFNames=N879_06045 {ECO:0000313|EMBL:ERI35083.1};
OS   Alcaligenes sp. EGD-AK7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=1386079 {ECO:0000313|EMBL:ERI35083.1, ECO:0000313|Proteomes:UP000016497};
RN   [1] {ECO:0000313|EMBL:ERI35083.1, ECO:0000313|Proteomes:UP000016497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-AK7 {ECO:0000313|EMBL:ERI35083.1};
RX   PubMed=24407646;
RA   Sagarkar S., Bhardwaj P., Yadav T.C., Qureshi A., Khardenavis A.,
RA   Purohit H.J., Kapley A.;
RT   "Draft genome sequence of atrazine-utilizing bacteria isolated from Indian
RT   agricultural soil.";
RL   Genome Announc. 2:e01149-13(2014).
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:ERI35083.1}.
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DR   EMBL; AVOG02000001; ERI35083.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1YJ19; -.
DR   PATRIC; fig|1386079.3.peg.1161; -.
DR   Proteomes; UP000016497; 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:UP000016497}.
FT   DOMAIN          12..375
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          422..500
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   518 AA;  56142 MW;  C0E39016F1AF49EF CRC64;
     MLGALARTTQ VDMVVVGGGA TGLGVALDAA LRGLSVVVLE AWDFAKGTSS RATKLVHGGV
     RYLAQGNVSL VREALRERMH LLSNAPHLAQ RLPFVMPSYK CWETPFYGVG LMAYDGLAGR
     EGLGHTQFLS ASKIRQLLPG ARQSGLKGGV KYWDGQFDDA RLALALARTA ALNGALLINY
     CPVVDVMHSE GKVCGVRCQD KESGQTYEIQ SKCVVNATGV WVDQVRQLDA QEAGRELRPM
     VSPSQGVHLV VDQEFLPGEH ALLVPRTKDG RVLFAVPWLG KLILGTTDTP RDDIPLEPRP
     LAQEVDFILK ESANYLQKAP TVRDVRSIWV GLRPLVRPAA ESAAGQTQSI SREHSITVSA
     NGLLTVTGGK WTTYRAMAED VLERCQQSGL LGPLPACRTQ EQRLVGASYV GDRRSLGRTA
     GLDAYGSEAD WVQTLPGADQ ELAPGLSVAM VRFACRFEYA RTVEDMLARR SRLLFLDARL
     AQSLAPAVAA IMEEETGRSP ELGAFLELAE QYATVPTR
//
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