ID W3REV8_9BRAD Unreviewed; 517 AA.
AC W3REV8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=X566_18205 {ECO:0000313|EMBL:ETR74753.1};
OS Afipia sp. P52-10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR74753.1, ECO:0000313|Proteomes:UP000018975};
RN [1] {ECO:0000313|Proteomes:UP000018975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX PubMed=25874801;
RA Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA Weingartl H.;
RT "Identification of a novel afipia species isolated from an Indian flying
RT fox.";
RL PLoS ONE 10:E0121274-E0121274(2015).
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:ETR74753.1}.
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DR EMBL; AZSJ01000007; ETR74753.1; -; Genomic_DNA.
DR RefSeq; WP_034469977.1; NZ_AZSJ01000007.1.
DR AlphaFoldDB; W3REV8; -.
DR STRING; 1429916.X566_18205; -.
DR PATRIC; fig|1429916.3.peg.3683; -.
DR eggNOG; COG0578; Bacteria.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000018975; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018975}.
FT DOMAIN 10..366
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 391..487
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 517 AA; 57019 MW; 67F105CF0C084EAC CRC64;
MDQISDQVYD IAIIGGGING CGIARDAAGR GLKVVLCEMD DLASGTSSWS TKLIHGGLRY
LEYYEFRLVR EALMEREVLW RIAPHIIHPL RLVLPHHAGL RPAWLLRLGL FLYDHLGGRK
RLPPTRTIDL AKDPLGKPLA AGFKRGFEYS DCTVDDARLV ILNARDAADH GAQILTRARA
VRINRGNGAW DITVEDHVTP NPRSIRARTI VNAAGPWVND VLSLSSIGGA KARVRLVQGS
HIVVPKLYDH DRAYMFQNAD GRIIFVIPYQ QDFTLIGTTD RDYDGDPAAV SITQDEISYL
CASASDYLAK PITPKQIVWS YAGVRPLYDD GASEAKAATR DYVFELDVDG GLPMLSIFGG
KITTYRRLAE EALERLAPYL PQSTGRHPGW TAEQPLPGGD FDTAVLPAVI NDLRANWPFL
TPSHASRLAT AYGTRAGALL DQAKTFTDLG QHFGATLTEA EIRFLIATEW AVTPDDILWR
RSKLGLRLSA LERKSLENWL ATHGSRPSSS PKIGKTL
//
