ID A0A0H5P6H5_NOCFR Unreviewed; 514 AA.
AC A0A0H5P6H5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-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 Name=glpD_1 {ECO:0000313|EMBL:CRY78121.1};
GN ORFNames=ERS450000_02764 {ECO:0000313|EMBL:CRY78121.1};
OS Nocardia farcinica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=37329 {ECO:0000313|EMBL:CRY78121.1, ECO:0000313|Proteomes:UP000057820};
RN [1] {ECO:0000313|Proteomes:UP000057820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11134 {ECO:0000313|Proteomes:UP000057820};
RG Pathogen Informatics;
RL Submitted (MAR-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}.
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DR EMBL; LN868938; CRY78121.1; -; Genomic_DNA.
DR RefSeq; WP_060592829.1; NZ_UGVK01000001.1.
DR AlphaFoldDB; A0A0H5P6H5; -.
DR KEGG; nfr:ERS450000_02764; -.
DR Proteomes; UP000057820; Chromosome 1.
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:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
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:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 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}.
FT DOMAIN 32..389
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 411..510
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 514 AA; 53736 MW; 7B2D6BDA0D9578A8 CRC64;
MTNHPERYGN SALDAARRTR ELHQLGDLGT VDVLVVGGGV TGAGAALDAA SRGLRTVLVE
RHDLAWGTSR WSSKLVHGGL RYLAGGRVGI ARESAIERGI LLGTVAPHLV RPLPQLVPLL
PGIGRAQQAL IRAGFLAGDA LRRSAGTPAA TLPRARRVAA AEALRLAPTV RRAGLRGGLQ
AWDGQLVDDA RLVVALARTA AAHGALVLTR VAAEAITGDS AVLRDTLTDE TLTVSAKAVI
NATGVWADQL DPSISLRPSR GTHLVFAAEA FAGLSASLTV PVPGSVGRFV FAFPAAHNRV
YLGLTDEDAP GPVPDEPQPT DAEVDFLLDT VNPALREPLT RADIRGRYAG LRPLLRTGDG
NTADISREHA VLHSPSGVFT IVGGKLTTYR RMAQDVVDAA VRAYRLPAGP CRTHTLPLVG
AVAGAARDRI AAPPLLVDRY GSEAPQILAL GERDPALREP VAPGLDVTAA EFAFARSHEA
ALTPDDLLDR RTRIGLVAAD RAAALAAATA AFEG
//
