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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//