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Database: UniProt
Entry: A0A370HBQ0_9NOCA
LinkDB: A0A370HBQ0_9NOCA
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ID   A0A370HBQ0_9NOCA        Unreviewed;       517 AA.
AC   A0A370HBQ0;
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_102498 {ECO:0000313|EMBL:RDI54373.1};
OS   Nocardia mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=279262 {ECO:0000313|EMBL:RDI54373.1, ECO:0000313|Proteomes:UP000255355};
RN   [1] {ECO:0000313|EMBL:RDI54373.1, ECO:0000313|Proteomes:UP000255355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44952 {ECO:0000313|EMBL:RDI54373.1,
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:RDI54373.1}.
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DR   EMBL; QQAZ01000002; RDI54373.1; -; Genomic_DNA.
DR   RefSeq; WP_068021136.1; NZ_QQAZ01000002.1.
DR   AlphaFoldDB; A0A370HBQ0; -.
DR   STRING; 1210089.GCA_001613165_03759; -.
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: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; 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          32..367
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          411..504
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   517 AA;  53981 MW;  C9FA023636EAB766 CRC64;
     MSSARGGFGD SALNAGRRSR ELQALGDGGD IDVLVVGGGV TGAGVALDAA ARGLRTVLVE
     KHDLAFGTSR WSSKLVHGGL RYLAGGGVGI AHESAVERDV LLTTTAPHLT RSIPQVVPLL
     PEVGRIQRAL VRTGFVAGDV LRRTAGTPAA VLPRSRRVAA AEALRLAPTL RRNGLRGGLL
     AWDGQLVDDA RLVVAIARTA AAYGASVLTR VAARQVTGES AQLCDALTGE TLTVRARSVI
     NAAGVWADRV DESIELRPSR GTHLVFDAAA FGGLTASLTV PIPGSTSRFV FAFPAAHGRV
     YLGLTDEDAP GPVPDEPRPT DGEIDFLLDT VNTVLREPLH RSDIRGSFAG LRPLLRTGGD
     DTSDISREHA VLHSPGGPVT VVGGKLTTYR QMAEDAVDAA VAHSGLTTTP CRTKRIPLVG
     AVSGAARDRI PAAPLLIERY GTEATGILEL IQRDPALGEP VAPGIDVLRA EFAYAVAHEG
     ALDEGDLLDR RTRIGLIEDD RAAALPAARL AVAPTRT
//
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