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Database: UniProt
Entry: A0A3A5MIL3_9MICO
LinkDB: A0A3A5MIL3_9MICO
Original site: A0A3A5MIL3_9MICO 
ID   A0A3A5MIL3_9MICO        Unreviewed;       580 AA.
AC   A0A3A5MIL3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase/oxidase {ECO:0000313|EMBL:RJT87749.1};
GN   ORFNames=D6T64_12855 {ECO:0000313|EMBL:RJT87749.1};
OS   Cryobacterium melibiosiphilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cryobacterium.
OX   NCBI_TaxID=995039 {ECO:0000313|EMBL:RJT87749.1, ECO:0000313|Proteomes:UP000272015};
RN   [1] {ECO:0000313|EMBL:RJT87749.1, ECO:0000313|Proteomes:UP000272015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hh39 {ECO:0000313|EMBL:RJT87749.1,
RC   ECO:0000313|Proteomes:UP000272015};
RA   Liu Q., Xin Y.-H.;
RT   "Novel species of Cryobacterium.";
RL   Submitted (SEP-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}.
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:RJT87749.1}.
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DR   EMBL; QZVS01000087; RJT87749.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A5MIL3; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000272015; 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: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}.
FT   DOMAIN          24..372
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          425..552
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   580 AA;  62621 MW;  C1EC5BFAD6DAECA3 CRC64;
     MQLNNPTPTP AAAENIQNRP NATVLIIGAG INGIATFRDL ALQGVSVAIV DRGDFVSGAS
     AASSHMIHGG VRYLENGEFR LVKESVTERN GLLKIAPHYV KPLQTTIPIF STFSGVMAAP
     LRFVTHKQGK THVERGAMLI KLGMMIYDSF SRDGGTVPRH EFTGRKRALA ALPQLNPTLK
     YTATYYDAAM HDPERLALDV LRDGLDAGTH ARAANYVEAI GMDENGVRLR DTVTGAEFSF
     AADVVVNTSG PWTDLTNEAL GQGSTFMGGT KGSHVVLDNP ELLAATGGRE IFFEHEDGRI
     VLIYPLKGRV LVGTTDLEHD MNDPIRVTEP EIDYFFDLVK TVFPTIAVDR SQIVYRFSGV
     RPLPRHDDEA PGFVSRDYRI EQAPLAHRTG TLLSLVGGKW TTFRALAENL SSQILELVGA
     ERTVSTEGLA IGGGKGFPAT DAAHLVWVTA HGDEIGRERA SELLARYGTR AELVIDFMTE
     PSAEPADAPL VHAPSYSRRE IEYLAATESV VRLIDVLLRR TSIAFVGGAT TAVIEELADV
     VAPVLGWDAA RRASEVDNAR GILTDVHGIT LSPVSAPVSA
//
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