ID A0A239CQH8_9BURK Unreviewed; 521 AA.
AC A0A239CQH8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=SAMN06265795_101575 {ECO:0000313|EMBL:SNS21921.1};
OS Noviherbaspirillum humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1688639 {ECO:0000313|EMBL:SNS21921.1, ECO:0000313|Proteomes:UP000198284};
RN [1] {ECO:0000313|EMBL:SNS21921.1, ECO:0000313|Proteomes:UP000198284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U15 {ECO:0000313|EMBL:SNS21921.1,
RC ECO:0000313|Proteomes:UP000198284};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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}.
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DR EMBL; FZOT01000001; SNS21921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239CQH8; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000198284; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198284}.
FT DOMAIN 11..331
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 387..491
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 521 AA; 57073 MW; E6F4BB01ECC2BD86 CRC64;
MREQAGDLQC DMLIVGGGVN GAGIARDAAG RGLSVVLCEK DDLAAHTSSA STKLIHGGLR
YLETYEFGLV RKALAEREVL LRSAPHIMWP LQFVMPHDAG QRPAWLIRAG LFLYDHLARR
ELLPASGAID LRRHEAGAPL KPAFERGFIY ADGWVDDARL VALNAVDASE KGAVILTRTR
CERLQREGGL WRAQLARADG SRIEVAARSV VNAAGPWAAD LLQQARPQGA QSALRLVKGS
HIIVPKLFDH PHAYLFQHPD GRIVFAIPYE HAFTLIGTTD IEYRGDPNQV CISEEEVGYL
CGLAQRYFRQ PVRAEDVVAT YSGVRPLLDD ASANASAVTR DYRLQLDRDG APLLSVLGGK
ITTFRKLAEQ AVDTLAPLLG CARPAWTEKA CLPGGDIFGP VPNNRAVQEF DGYLRSLQRR
YAWLPPALVA RYARAYGRRI ELLMEGRAEP AQMGEEILPG LYAAEVDYLM RREFAGCADD
ILWRRSKLGL HLPADAGSRL DAWIAARAGA TVLAPAANAV R
//
