ID A0A1Q3VWC4_9PROT Unreviewed; 528 AA.
AC A0A1Q3VWC4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:OJW52115.1};
GN ORFNames=BGO63_19790 {ECO:0000313|EMBL:OJW52115.1};
OS Candidatus Accumulibacter sp. 66-26.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1895689 {ECO:0000313|EMBL:OJW52115.1, ECO:0000313|Proteomes:UP000186203};
RN [1] {ECO:0000313|EMBL:OJW52115.1, ECO:0000313|Proteomes:UP000186203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=66-26 {ECO:0000313|EMBL:OJW52115.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJW52115.1}.
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DR EMBL; MKUH01000006; OJW52115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3VWC4; -.
DR STRING; 1895689.BGO63_19790; -.
DR Proteomes; UP000186203; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 22..384
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 419..503
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 528 AA; 56753 MW; 48B4B4971C4E6DA3 CRC64;
MMAKPLRRED DLAALRDGHP WDVLVIGGGA TGLGCAVDAA ARGYRTLLVE ARDFAAGTSS
RSTKLIHGGV RYLRQGDLVL VRQALRERAR LLHNAAHLVQ PLPFVIPAWS AIDRLFYAGG
LKLYDTLAGW RNLESSALLD RAETLAALPG LRRAGLTGGV RYWDGKFDDA RLAVALMRTA
AGLGATSLNY LPATQLIKAG GRIAGAWLRD AETGEGFEVR ARTVINATGV WADKVRRLDD
PNAAPLLTPS QGIHLVFDAD FLPGGNALLV PKTEDGRVVF AIPWQGRVLL GTTDTARPDL
PAEPQPLAGE IDFLLHAAAG VLERPPQRAD IRSVFAGLRP LLHPEHPQRA ADKSGTAALS
REHAVLVGDS GLVTVTGGKW TTYRRMAQEA VERAAELGGL HAAPCRTRDL KLHGCPPPTQ
AAGHDIYDSY GTDAPLLAML PGNDQHLHAG LPYTEAMVRF ALRYEAARTV EDILARRTRL
LFLDAQAAEA AIARVGEIVA EELAPPPERF AAMLAAARDS ARCFMPAQ
//
