ID G2I392_KOMMN Unreviewed; 520 AA.
AC G2I392;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN OrderedLocusNames=GLX_02850 {ECO:0000313|EMBL:BAK82697.1};
OS Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG 1693 /
OS Kondo 51) (Gluconacetobacter medellinensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=634177 {ECO:0000313|EMBL:BAK82697.1, ECO:0000313|Proteomes:UP000009044};
RN [1] {ECO:0000313|Proteomes:UP000009044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693
RC {ECO:0000313|Proteomes:UP000009044};
RX PubMed=22123756; DOI=10.1128/JB.06158-11;
RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., Hasegawa A.,
RA Otsuyama K., Matsushita K., Fujita N., Shirai M.;
RT "Complete genome sequence of NBRC 3288, a unique cellulose-nonproducing
RT strain of Gluconacetobacter xylinus isolated from vinegar.";
RL J. Bacteriol. 193:6997-6998(2011).
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; AP012159; BAK82697.1; -; Genomic_DNA.
DR RefSeq; WP_014104277.1; NC_016027.1.
DR AlphaFoldDB; G2I392; -.
DR STRING; 634177.GLX_02850; -.
DR KEGG; gxy:GLX_02850; -.
DR PATRIC; fig|634177.7.peg.316; -.
DR eggNOG; COG0578; Bacteria.
DR HOGENOM; CLU_015740_5_0_5; -.
DR Proteomes; UP000009044; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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}.
FT DOMAIN 19..340
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 399..498
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 520 AA; 57597 MW; 0342CE9AE2C1A2D8 CRC64;
MVSMDETLSP PPVQDSPFDL LVVGGGVNGT GIARDAAGRG ASVLLVEQDD LASYTSSAST
KLIHGGLRYL EYYEFRLVRE ALIERERLLR IAPHIIWPMR FVLPYTPQAR PAWMLRLGLF
LYDHLAPNMT LPKCKSLDFR TSSAGKPLNG KLARGFAYSD GWVQDSRLVV LNAMDAKARG
ADIRTRTRLV QARRVDGLWE AVIENTRDGS QQTVRAKIVV NAGGPWVSEV LRERAQVETT
KNVRLVKGSH IVVPRLFDGP QAYILQNPDK RIVFAIPYEQ KFTLIGTTDV PWTQAPGRVE
ISPDEISYLC ESVSRYFTKP VTPADVVWSY AGVRPLYDDA AKNASAVTRD YVLDVDTQGN
QAPMLSIFGG KITTFRRLAE HAIEKLQPFL PVLSAPGWTA DKVLPGGDLG EGGFEGAMGR
LAAKAPFLDQ QLCWRLVRNY GSRADVIVGD ARSMEDMGEQ FGGGLTAREV EYLIAHEWAQ
TTEDILWRRS RLGLHVTDED AGRLDTYLRG RQPVAAKAAS
//
