ID A0A0C5EAF7_9PSED Unreviewed; 512 AA.
AC A0A0C5EAF7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD {ECO:0000313|EMBL:AJO80346.1};
GN ORFNames=TO66_24920 {ECO:0000313|EMBL:AJO80346.1};
OS Pseudomonas sp. MRSN 12121.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1611770 {ECO:0000313|EMBL:AJO80346.1, ECO:0000313|Proteomes:UP000032239};
RN [1] {ECO:0000313|EMBL:AJO80346.1, ECO:0000313|Proteomes:UP000032239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN12121 {ECO:0000313|EMBL:AJO80346.1,
RC ECO:0000313|Proteomes:UP000032239};
RA McGann P., Snesrud E., Ong A.C., Clifford R., Kwak Y.I., Steele E.D.,
RA Rabinowitz R., Waterman P.E., Lesho E.;
RT "Allelic Variants of blaVIM Reside on Diverse Mobile Genetic Elements in
RT Gram-negative Clinical Isolates from the USA.";
RL Submitted (FEB-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010892; AJO80346.1; -; Genomic_DNA.
DR RefSeq; WP_044464772.1; NZ_CP010892.1.
DR AlphaFoldDB; A0A0C5EAF7; -.
DR KEGG; psem:TO66_24920; -.
DR PATRIC; fig|1611770.3.peg.5159; -.
DR HOGENOM; CLU_015740_5_0_6; -.
DR Proteomes; UP000032239; 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.
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:UP000032239}.
FT DOMAIN 16..368
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 390..499
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 512 AA; 56841 MW; FF0A89B351A512FE CRC64;
MPTSTLPAPP LAEIYDIAVI GGGINGVGIA ADAAGRGLSV FLCEKDDLAS HTSSASSKLI
HGGLRYLEHY EFRLVREALA EREVLLAKAP HIVKPMRFVL PHRPHLRPAW MIRAGLFLYD
HLGKREKLAG SKSLKFGADS PLKAEISKGF EYSDCWVDDA RLVVLNAMAA REKGAHVHTQ
TRCVSARRSK GMWHLHLERA DGSLFSIRAK ALVNAAGPWV AKFIKDDLKL DSPYGIRLIQ
GSHLIVPKLY EGEHAHILQN EDQRIVFTIP YLNHFTLIGT TDREYTGDPA KVAITEGETD
YILKVVNAHF KKQLGRQDIV HTYSGVRPLC NDESDNPSAV TRDYTLALSG GTDEAPLLSV
FGGKLTTYRK LAESAMAQLA PFFKGIKPSW TAHSTLPGGE DMSTPQALAE AIRQKFDWIP
SEIARRWATS YGSRTWRLLE GVHSLSDLGE HLGGGLYTRE VDYLCSEEWA VNAQDILWRR
SKLGLFTTAA EQENLQQYLQ KVEQNRAKIE AA
//
