ID Q2GC89_NOVAD Unreviewed; 489 AA.
AC Q2GC89;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE SubName: Full=Homodimeric glycerol 3-phosphate dehydrogenase (Quinone) {ECO:0000313|EMBL:ABD24534.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:ABD24534.1};
GN OrderedLocusNames=Saro_0085 {ECO:0000313|EMBL:ABD24534.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD24534.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) 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}.
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DR EMBL; CP000248; ABD24534.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GC89; -.
DR STRING; 279238.Saro_0085; -.
DR KEGG; nar:Saro_0085; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_0_5; -.
DR Proteomes; UP000009134; Chromosome.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
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:InterPro.
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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABD24534.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT DOMAIN 6..317
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 374..482
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 489 AA; 54112 MW; 8ACF77A3C6E66826 CRC64;
METPYDLAVI GGGVNGAAIA RDACGRGLSV LLLERGDLAQ GTSSASTKLI HGGLRYLEHR
EFALVAEALH ERETLWRQAP HIIWPMRFVL PIVPEGRPWW MLRAGLWLYD RIGGRKALPP
ASRVRLDGRM GLQPEIRRGY EYSDCWVDDA RLVVLLARDA ADRGAEVRTR CPVTALRREG
HLWRIEAGGD VFHAAMTVNA AGPQVGEIMD RAHAPRPALL RRVRGSHIVV PRLHDDPRAL
FLQLADGRIY FAIPWQYAFT LIGTTDSEEG ADADPPHATE EEIAYLLDAA NHYFRRSLRR
EDVVWTYAGV RLLADDGSGR PEAATRGYRL EVDRGRDRHS APMLSVLGGK ITTHRTLAEA
ALERLGVTDN AGWTASAPLP GGDFTPDGLD EADNLAPVEQ EIAAQAQQLS RPTIHRLARA
YGTEALGFVR GDMGRHIGQG FTEAELDHLT GREWAQTAED VLWRRSKLGM WFSAEEVAAL
KAALGEEVR
//
