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Database: UniProt
Entry: A0A1Y2R311_9BURK
LinkDB: A0A1Y2R311_9BURK
Original site: A0A1Y2R311_9BURK 
ID   A0A1Y2R311_9BURK        Unreviewed;       526 AA.
AC   A0A1Y2R311;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OSZ74010.1};
GN   ORFNames=CAP37_00550 {ECO:0000313|EMBL:OSZ74010.1};
OS   Hydrogenophaga sp. IBVHS1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1985169 {ECO:0000313|EMBL:OSZ74010.1, ECO:0000313|Proteomes:UP000194358};
RN   [1] {ECO:0000313|EMBL:OSZ74010.1, ECO:0000313|Proteomes:UP000194358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVHS1 {ECO:0000313|EMBL:OSZ74010.1,
RC   ECO:0000313|Proteomes:UP000194358};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-2017) 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:OSZ74010.1}.
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DR   EMBL; NFUU01000001; OSZ74010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2R311; -.
DR   STRING; 1985169.CAP37_00550; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000194358; 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:UP000194358}.
FT   DOMAIN          17..383
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          433..509
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   526 AA;  56253 MW;  7411F13D53A20E2F CRC64;
     MKRAELIASL TASPDFDLAI VGGGATGLGV ALDAALRGFS VVLLESHDFA GGTSSRSTKL
     LHGGVRYLAQ GNLALVREAL AERATVLRIA PHLAQPLPFV MPSYRWWQTP FYGLGLKLYD
     LLAGSAGLGR TEFLSRAQAL QALPGVNPKG LRGGVKYWDG QFDDARLALA LARSAAAAGA
     RVLNYAEVTA IRQSTDGQNP MSTLEATDRR TGTALTLRAR CVVNATGVWV DALRDRTQPP
     ASTEGRPSQM VSPSQGVHVV VDREFMPGGH ALLVPRTRDG RVLFAVPWLG KLVLGTTDTP
     RKDLPREPDA FAEELEFILA EASQALGRPV RKADIRSLWV GLRPLVAAPA SAEGGTQALS
     REHTIVVDPN GLVTVTGGKW TTYRAMAEDV LERCFATNLL PRRAGSRSDN HRLLGAGLTG
     LPATPLHAAP GMHLYGSEWA EVQKCQGLGN LLGMGLNEAM VRHAAREEFA QTVEDVLARR
     WRVLFLDARQ AALMAPAVAA ILAEELGGDP DLAGFLALCE RYLPAV
//
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