ID A0A370GL70_9NOCA Unreviewed; 558 AA.
AC A0A370GL70;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=DFR68_11792 {ECO:0000313|EMBL:RDI44475.1};
OS Nocardia mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=279262 {ECO:0000313|EMBL:RDI44475.1, ECO:0000313|Proteomes:UP000255355};
RN [1] {ECO:0000313|EMBL:RDI44475.1, ECO:0000313|Proteomes:UP000255355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44952 {ECO:0000313|EMBL:RDI44475.1,
RC ECO:0000313|Proteomes:UP000255355};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDI44475.1}.
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DR EMBL; QQAZ01000017; RDI44475.1; -; Genomic_DNA.
DR RefSeq; WP_068025059.1; NZ_QQAZ01000017.1.
DR AlphaFoldDB; A0A370GL70; -.
DR STRING; 1210089.GCA_001613165_05294; -.
DR OrthoDB; 9766796at2; -.
DR Proteomes; UP000255355; Unassembled WGS sequence.
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; 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:UP000255355}.
FT DOMAIN 23..371
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 398..520
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 558 AA; 60072 MW; 224CFAD1E3F0E4B5 CRC64;
MTTQLDSQYR AEGLNSLGRK DIDVLVIGGG VVGAGAALDA ASRGLTTVVV EARDWAAGTS
SRSSKLIHGG LRYLEQLDFA LVREALKERG LLLNRLAPHL VHPVSFLFPL QHHWERPYIG
AGVALYDTLG GARALPMHKH LSRTRALELA PALRADAMTG AIRYFDAQVD DARHTMMLAR
TAAQHGATVL TRTRVTGLLR EGEQVVGATV TDRETGRSYD VRARSVISAT GVWTDEMNAM
TGVDFPFHVR MSKGVHIMVP RARLNLGTGL IMKTEKSVLF VIPWREHWII GTTDTDWSLD
RNHPVATATD VRYILDHLNS LLREPISEDD IVGTYAGLRP LLSGASSDTS KLSREHAVAE
PVPGLFVVAG GKYTTYRVMA ADVVDAAVAG FGQGMAPSVT QNLPLLGAVG YHEMLDDVEG
VAARAGLPVE TISHLLERYG ALTTELIGMI DAAPELGMPL PGASEYLGAE AVYAVTHEGA
LHLDDILTRR TRISIEVPDR GLTAAVAVAD LVAPHLGWDE PAKAAELARY RDRVQAELAA
NEATDDEAAN TARLVAVS
//
