ID A0A097ECV2_9SPHN Unreviewed; 493 AA.
AC A0A097ECV2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=MC45_02155 {ECO:0000313|EMBL:AIT05402.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT05402.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT05402.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT05402.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-2014) 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; CP009571; AIT05402.1; -; Genomic_DNA.
DR RefSeq; WP_038658941.1; NZ_CP009571.1.
DR AlphaFoldDB; A0A097ECV2; -.
DR STRING; 1549858.MC45_02155; -.
DR KEGG; stax:MC45_02155; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_0_5; -.
DR Proteomes; UP000033200; Chromosome.
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:UP000033200}.
FT DOMAIN 10..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 388..479
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 493 AA; 53851 MW; DBD42DBC879B0AF5 CRC64;
MERGPDESVD VLVVGGGING TGIARDAAGR GLSVLLVEQD DLANHTSSAS TKLIHGGLRY
LEYGEFRLVR EALIERERLW GMAPHIIWPL RFVLPQTHSP RPAWMVRAGL FLYDHLGGRR
KLPGTQSVAL ARSPFGQGLS ERVGKAFVYS DCWVEDSRLV VLNARDAAER GARIATRTRL
VRAQRGADGW TAEIADKDGH VRMVRARALV NAAGPWVADV LGRTAGARND RGVRLVKGSH
IVVPQLYEGD HAFILQNDDR RIVFAIPYEG RFTLVGTTDA AWDAPPGRAA IDAAETHYLL
DTIARYFEHR VEADDIVWSY AGIRPLYDDK AANASAVTRD YVLDLDAGEG QAPMLSVYGG
KITTYRKLAE HALRDLAPLL GSQAPAWTAG AVLPGGDLPD ADFVGFLTGL QARYPEVSRD
LLRRLAHAYG TRATAILDRD PGQDLGGGLF TTEVDYLVAQ EWAQTAEDVL WRRSKLGLHV
PAGTAERLAA YLG
//
