ID Q2K200_RHIEC Unreviewed; 582 AA.
AC Q2K200;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Probable glycerol-3-phosphate dehydrogenase protein {ECO:0000313|EMBL:ABC93115.1};
DE EC=1.1.5.3 {ECO:0000313|EMBL:ABC93115.1};
GN OrderedLocusNames=RHE_PB00073 {ECO:0000313|EMBL:ABC93115.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid p42b {ECO:0000313|EMBL:ABC93115.1,
OG ECO:0000313|Proteomes:UP000001936}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC93115.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:ABC93115.1, ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000135; ABC93115.1; -; Genomic_DNA.
DR RefSeq; WP_011427537.1; NC_007763.1.
DR AlphaFoldDB; Q2K200; -.
DR KEGG; ret:RHE_PB00073; -.
DR HOGENOM; CLU_015740_5_1_5; -.
DR Proteomes; UP000001936; Plasmid p42b.
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; 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.
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:ABC93115.1}; Plasmid {ECO:0000313|EMBL:ABC93115.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936}.
FT DOMAIN 17..398
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 422..541
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 582 AA; 63635 MW; 177F09C37CEB0ECB CRC64;
MNRVETMDGL RQSPKVDVCV LGGGINGLSV FRELALQGVN VLLVEQGDYC SGASAALSRM
VHGGLRYLEN GEFSLVQESL FERDRLLRNA PHYVAPLPTT VPVFDIFSGL ANGIVRFLGL
TRRPSRRGAV AIKTGLAIYD FLTRKRALMP RHQFRGRRAT LSKWPALNPG IRSSATYYDA
WVSHPERIGI ELLRDGLSAG PNARALNYAT IAQAGAGDFQ LCDGVAGETF RIQPRLVVNA
TGGWIDIANG SLFSEGTRPE PLMGGTKGSH LIIDNPALRD MLDGHMIYYE NEDGRICILF
PYLGKVLVGS TDIRVDDPGT VRCEPDERDY ILQSLAFVLP GIGIRPEEIV FQFAGVRPLP
ASKDSFTGRI PRDHFCTVIE GHEDGPPVLC MIGGKWTTFR SFGELAADMV LERLGWPRRI
DTAERAFGGG RAFPKDGGGW VRDLAASTGI SIDRAAILFE RYGTDAEHVA GFIAAGPDHP
LPHAGYSLRE IQYLIGAEAV EHLDDLLLRR TTLAISGELS LDMADAVLAL LAAARGWSAE
RAAEERIRFL TIMRERHGVA EATLSARNER RSELCETTAR SG
//
