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Database: UniProt
Entry: A0A261VME9_9BORD
LinkDB: A0A261VME9_9BORD
Original site: A0A261VME9_9BORD 
ID   A0A261VME9_9BORD        Unreviewed;       534 AA.
AC   A0A261VME9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OZI75027.1};
GN   ORFNames=CAL22_11480 {ECO:0000313|EMBL:OZI75027.1};
OS   Bordetella genomosp. 12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463035 {ECO:0000313|EMBL:OZI75027.1, ECO:0000313|Proteomes:UP000216429};
RN   [1] {ECO:0000313|EMBL:OZI75027.1, ECO:0000313|Proteomes:UP000216429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU6712 {ECO:0000313|EMBL:OZI75027.1,
RC   ECO:0000313|Proteomes:UP000216429};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
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:OZI75027.1}.
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DR   EMBL; NEVU01000002; OZI75027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261VME9; -.
DR   Proteomes; UP000216429; 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}.
FT   DOMAIN          26..387
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          435..514
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   534 AA;  57219 MW;  B25CF2EFEEEEECE3 CRC64;
     MNPSPSPLMP TRADLLARLE SSEPWDVIVI GGGATGLGTA VDAASRGFRT LLVEGADFAK
     GTSSKATKLV HGGVRYLAQG NVSLVREALH ERGLLARNAP HLAWPLGFVV PAYSLLDQPF
     YGVGLKLYDM LAGKLNLAPS RWLSARETLT HASTLAPAVK GQRLRGGVLY YDGQFDDARL
     ATALMRTLFD LGGTSVNYVK VTGLTRDAQG RIDGVQTQDS IDGGHYTVHG KCVVNATGVW
     VDAVRRMDDP AAQTMVAPSQ GVHLTLPREF LPGDEAILVP KTDDGRVLFM VPWNGHTIVG
     TTDTARTDLP SDPRPLPGEV DFILETAARY LTRKPTRADV TSVWAGLRPL VKATGEASTK
     SLSREHTILV SKAGLITVTG GKWTTYRRMA QDVVDTAISK QLLPQAMCRS AELRLHGAPA
     PDAPLPAAQG TPDSYYGTDL PALRALPGAD RMLVKASGLT EAHVRFAARH ELAQTVEDVL
     ARRNRALFLD AAAAQLAAPE VARVLAEELG RDAAWQGRTL ADFDAVAATF RLPE
//
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