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Database: UniProt
Entry: A0A221T097_9DEIO
LinkDB: A0A221T097_9DEIO
Original site: A0A221T097_9DEIO 
ID   A0A221T097_9DEIO        Unreviewed;       520 AA.
AC   A0A221T097;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:ASN82332.1};
GN   ORFNames=DFI_14170 {ECO:0000313|EMBL:ASN82332.1};
OS   Deinococcus ficus.
OG   Plasmid pdfi1 {ECO:0000313|Proteomes:UP000259030}.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=317577 {ECO:0000313|EMBL:ASN82332.1, ECO:0000313|Proteomes:UP000259030};
RN   [1] {ECO:0000313|EMBL:ASN82332.1, ECO:0000313|Proteomes:UP000259030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-FR2-10 {ECO:0000313|EMBL:ASN82332.1,
RC   ECO:0000313|Proteomes:UP000259030};
RC   PLASMID=pdfi1 {ECO:0000313|Proteomes:UP000259030};
RA   Wu K.-M., Liao T.-L., Liu Y.-M., Young C.-C., Tsai S.-F.;
RT   "The complete genome sequence of Deinococcus ficus isolated from the
RT   rhizosphere of the Ficus religiosa L. in Taiwan.";
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}.
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DR   EMBL; CP021082; ASN82332.1; -; Genomic_DNA.
DR   RefSeq; WP_027463633.1; NZ_CP021082.1.
DR   AlphaFoldDB; A0A221T097; -.
DR   STRING; 317577.GCA_000419625_02829; -.
DR   KEGG; dfc:DFI_14170; -.
DR   Proteomes; UP000259030; Plasmid pdfi1.
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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Plasmid {ECO:0000313|EMBL:ASN82332.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000259030}.
FT   DOMAIN          20..378
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          392..500
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   520 AA;  56551 MW;  A72CE2B09BAFBF7F CRC64;
     MPQDPRSALL SAATTPQTWD ILVIGGGASG LGTAVEAATR GHRTLLLEGH DYAKGTSSRS
     TKLVHGGVRY LAQGNVSLVR EALRERGLLR KNAPHLVHDL GFLVPAYDWW AGPFYGIGLK
     LYDLLAGKLN LGSSKYLDKT EALARTSTLK PDGLRGGILY FDGQFDDARL AITLLRTFED
     HGGVALNYAP VVGLIMEEGK VVGARFRDAE TGHEHDVRAR AVVNATGVWV DDIRRMEKPD
     AEPMLSPSQG VHVVVDRHFL PGDNAIMIPR TDDGRVLFAV PWHGSVVIGT TDTPVPQASF
     EPRPLEEEIA FILSTAGRYL SPAPTKSDVR SVYVGLRPLV KSEQTDGAGS TASLSRDHII
     RISDGGLITL TGGKWTTYRR MGEDTINRAE PLAGLAQRLT VTPGLHLHGW SEEPRDDHWR
     VYGSDAAQVQ SLPGAGTPLH PDLPYTEAEL RWGVRFEGAR TVEDLLARRT RALLLNARAS
     SETAPRAAAI LAEELGRDAA WAELQTQSYQ DLARGYQLPS
//
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