ID A0A1S1NH59_9MYCO Unreviewed; 512 AA.
AC A0A1S1NH59;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN ORFNames=BKN37_16370 {ECO:0000313|EMBL:OHV01895.1};
OS Mycobacterium talmoniae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1858794 {ECO:0000313|EMBL:OHV01895.1, ECO:0000313|Proteomes:UP000179734};
RN [1] {ECO:0000313|EMBL:OHV01895.1, ECO:0000313|Proteomes:UP000179734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE-TNMC-100812 {ECO:0000313|Proteomes:UP000179734};
RA Greninger A.L., Elliott B., Vasireddy S., Vasireddy R.;
RT "Genome sequence of Mycobacterium talmonii.";
RL Submitted (OCT-2016) 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:OHV01895.1}.
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DR EMBL; MLQM01000093; OHV01895.1; -; Genomic_DNA.
DR RefSeq; WP_071027724.1; NZ_MLQM01000093.1.
DR AlphaFoldDB; A0A1S1NH59; -.
DR Proteomes; UP000179734; 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.
DR PROSITE; PS00387; PPASE; 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:UP000179734}.
FT DOMAIN 26..381
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 405..499
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 512 AA; 53268 MW; 2AEE895FDC7ABDFF CRC64;
MSDANALNAT RRTVELMALA DGDPVDVVVI GGGITGAGVA LDAVTRGLRV VLVEKHDLAF
GTSRWSSKLV HGGLRYLATG NVGIARRSAV ERGILMTRNA PHLVRAMPQL VPLLDSMGRG
QRALVRAGFV AGDVLRRLAG TPSAILPGSR RIPPARVLDL APTVRRDGLD GGLLAYDGQL
IDDARLVTAV ARTAASYGAR ILTYAAASRV TGTSVRLTDQ RSGESFDVSA RAVINATGVW
AGEIDPALTL RPSRGTHLVF AAEAFGNPTA ALTVPIPGEL NRFVFAMPEQ LGRVYLGLTD
EEAPGPIPDV PQPSSSETAF LLDTVNTALG TALGAADVIG SYAGLRPLID TGQGRTADVS
REHAVVESES GVLSVIGGKL TEYRYMAEDV LDRAVAARGL SAGGCRTRDL PLVGALSNPG
TATPLTTGLP ASLVARYGAE AGNVVATATC ERPGDPVADG IDVIRAEFEY AVTHEGALGV
DDILDRRTRI GLVPADRERV VAVAQEFVAS GC
//
