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Database: UniProt
Entry: A0A2S0WXF7_9MICO
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Original site: A0A2S0WXF7_9MICO 
ID   A0A2S0WXF7_9MICO        Unreviewed;       583 AA.
AC   A0A2S0WXF7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AWB95960.1};
GN   ORFNames=DCE93_10035 {ECO:0000313|EMBL:AWB95960.1};
OS   Agromyces badenianii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=2080742 {ECO:0000313|EMBL:AWB95960.1, ECO:0000313|Proteomes:UP000244729};
RN   [1] {ECO:0000313|EMBL:AWB95960.1, ECO:0000313|Proteomes:UP000244729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30A {ECO:0000313|Proteomes:UP000244729};
RA   Li J.;
RL   Submitted (APR-2018) 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; CP028913; AWB95960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S0WXF7; -.
DR   KEGG; agm:DCE93_10035; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000244729; Chromosome.
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: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   Reference proteome {ECO:0000313|Proteomes:UP000244729}.
FT   DOMAIN          33..379
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          434..557
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  63431 MW;  E24DCACCC577B6BF CRC64;
     MSPQQTNPNQ PRPHSSGERA DVAAIRTRPT ASVLVIGAGI NGIATFRDLA LQGVDVVLVD
     RGDFVSGASA ASSHMIHGGI RYLENGEFRL VKESVTERNA LIRIAPHYVK PLETTVPIFS
     TFSGILSAPL RFLTHKSGKP TERGAALIKT GLVIYDSFSR DGGSVPRHRF HGRKRSLAEL
     PALNHDIKYT ATYYDASMHD PERLALDVLF DGLAAGGHAR AANYLEAVGM GEHGVRLRDT
     LTGAEFEVAA DVVVNTSGPW TDLTNEELGR PTAFMGGTKG SHIVLDNDEL LAATGGREIF
     FEHEDGRIVL IYPLKGKVMV GTTDLEHDMR EPAVCTEAEV DYFFDLIAHV FPAVPVDRSQ
     IVYRFSGVRP LPRHDDEAPG FVSRDYRIER ADLPELPGTT LLSLVGGKWT TFRALAEHLS
     NEVLELLGRE RTRSTAGVAI GGGAGYPTTD DARRIWTVSH GDEVGRARAE ELLERYGTRA
     EAFIASIEGA RDEPLEHHVG YSRREIAWLV GGERVVHLAD VVLRRTSIAF TGAITAPLLD
     ELAEIAGAEL GWDAERRATE VAATRELLAA RHGVELEASA TLV
//
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