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Database: UniProt
Entry: A0A3M6Q9Y1_9BURK
LinkDB: A0A3M6Q9Y1_9BURK
Original site: A0A3M6Q9Y1_9BURK 
ID   A0A3M6Q9Y1_9BURK        Unreviewed;       545 AA.
AC   A0A3M6Q9Y1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Glycerol-3-phosphate dehydrogenase/oxidase {ECO:0000313|EMBL:RMW99987.1};
GN   ORFNames=EBQ25_05910 {ECO:0000313|EMBL:RMW99987.1};
OS   Allofranklinella schreckenbergeri.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Allofranklinella.
OX   NCBI_TaxID=1076744 {ECO:0000313|EMBL:RMW99987.1, ECO:0000313|Proteomes:UP000267035};
RN   [1] {ECO:0000313|EMBL:RMW99987.1, ECO:0000313|Proteomes:UP000267035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML161473 {ECO:0000313|EMBL:RMW99987.1,
RC   ECO:0000313|Proteomes:UP000267035};
RA   Bernier A.-M., Bernard K.;
RT   "Comamonadaceae CDC group NO-1 genome sequencing and assembly.";
RL   Submitted (OCT-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:RMW99987.1}.
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DR   EMBL; RDQL01000006; RMW99987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M6Q9Y1; -.
DR   Proteomes; UP000267035; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267035}.
FT   DOMAIN          27..392
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          415..528
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   545 AA;  58599 MW;  38FE3FB8D138C43B CRC64;
     MTLATQAPLP TQRPQLLRRL ADTPAFDVLV IGGGATGLGV ALDAVTRGLS VALVEAHDFA
     KGTSSRATKL VHGGVRYLAQ GNVALVREAL HERAALLENA PHLAQRLPFI MPSYKLWETP
     FYGTGLRMYD ALAGRDGLGA TQCLSRERVQ ALAPNVLAQG LRGGVLYWDG QFDDARLALA
     LARTAALHGA QVLNYLRVEQ LLHASDGRVC GAEVVDQETH ARFAIQATCV INATGVWVDA
     LRQLDEAGRQ GSAAVPPMVS PSQGTHIVVD RQFWPSEHAL LVPKTRDGRV LFAVPWLGSV
     ILGTTDRARS DLPLEPRPQA EEIGFILQEA ARYLAQPPKL EDVRSSWAGM RPLVRPVAAD
     GSSTKTLSRE HTIHTSASGM VTVTGGKWTT YRAMAEDVIR HAQLAGVLPA KLPPSQTRHL
     PLVGSPQPRE GAMQAAAMPQ SSLHSVPGLA VYGSEADYVR TLQGSDVELS PAHQLSEAMV
     RYAVRHEYAR SVEDVLARRS RLLFLDAKAA AALAPRVAQI MGEELGHSVD AAVFQQLAQQ
     YADAG
//
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