ID A0A0R2TAP6_9GAMM Unreviewed; 523 AA.
AC A0A0R2TAP6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=ABR85_04155 {ECO:0000313|EMBL:KRO84039.1};
OS OM182 bacterium BACL3 MAG-120619-bin3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; OMG group; OM182 clade.
OX NCBI_TaxID=1655593 {ECO:0000313|EMBL:KRO84039.1, ECO:0000313|Proteomes:UP000051242};
RN [1] {ECO:0000313|EMBL:KRO84039.1, ECO:0000313|Proteomes:UP000051242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL22 MAG-120619-bin3 {ECO:0000313|EMBL:KRO84039.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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:KRO84039.1}.
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DR EMBL; LICD01000012; KRO84039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TAP6; -.
DR Proteomes; UP000051242; Unassembled WGS sequence.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.250.1890; -; 1.
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; PS00977; FAD_G3PDH_1; 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 ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 9..327
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 383..512
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 523 AA; 57149 MW; C7ED06671A1D1682 CRC64;
MTDSPVVTDL LVIGGGINGA GVAADAAGRG LSVMLIEKGD LASGTSSWST KLIHGGLRYL
EFYEFGLVRK ALLERDVLTK AAPHIIRPLA FNIPQLPISR PAWMLRAGLF LYDFLAKSAI
FKHSRAIRFG NDSPLNGGIT KGFEYWDAQV DDSRLVVLNA QQAAEHGADV RTYTECVALE
EGKGHWIVTL REASSGIEQV VHAKAVVNAA GPWVARLLEK LFAKKPPLDT RLVKGSHIVV
PRLHCGDQAF MLQHTDGRVI FVIPYLDDYS LIGTTEAEFD GVLETVHIDE DEIAYLIEVA
NGYFKRQLSR DDVISTYSGV RPLIDEEGKD ATKVSRDYHL EPHKSAVPLL SIYGGKVTTY
RTLAEDVMKA LAPTFPKMGA PWTKQAPLPG GNYSAQFGGK NGELQSGRDA KASAEDEATL
SALLSAQAPW LQVSLLKRWL QTYGTETQTL LGDASSASDL GMHLGADLYS REVDYLIAHE
WARNPDDILW RRTKLGYLFD ERGKAVLADY ITTVRAAAAK GAG
//
