ID G0TNF0_MYCCP Unreviewed; 516 AA.
AC G0TNF0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN Name=glpD1 {ECO:0000313|EMBL:CCC44603.1};
GN OrderedLocusNames=MCAN_22711 {ECO:0000313|EMBL:CCC44603.1};
OS Mycobacterium canettii (strain CIPT 140010059).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1048245 {ECO:0000313|EMBL:CCC44603.1, ECO:0000313|Proteomes:UP000008896};
RN [1] {ECO:0000313|EMBL:CCC44603.1, ECO:0000313|Proteomes:UP000008896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44603.1,
RC ECO:0000313|Proteomes:UP000008896};
RX PubMed=22389744; DOI=10.1371/journal.pntd.0001552;
RA Bentley S.D., Comas I., Bryant J.M., Walker D., Smith N.H., Harris S.R.,
RA Thurston S., Gagneux S., Wood J., Antonio M., Quail M.A., Gehre F.,
RA Adegbola R.A., Parkhill J., de Jong B.C.;
RT "The Genome of Mycobacterium Africanum West African 2 Reveals a Lineage-
RT Specific Locus and Genome Erosion Common to the M. tuberculosis Complex.";
RL PLoS Negl. Trop. Dis. 6:e1552-e1552(2012).
RN [2] {ECO:0000313|EMBL:CCC44603.1, ECO:0000313|Proteomes:UP000008896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIPT 140010059 {ECO:0000313|EMBL:CCC44603.1,
RC ECO:0000313|Proteomes:UP000008896};
RX PubMed=23291586; DOI=10.1038/ng.2517;
RA Supply P., Marceau M., Mangenot S., Roche D., Rouanet C., Khanna V.,
RA Majlessi L., Criscuolo A., Tap J., Pawlik A., Fiette L., Orgeur M.,
RA Fabre M., Parmentier C., Frigui W., Simeone R., Boritsch E.C., Debrie A.S.,
RA Willery E., Walker D., Quail M.A., Ma L., Bouchier C., Salvignol G.,
RA Sayes F., Cascioferro A., Seemann T., Barbe V., Locht C., Gutierrez M.C.,
RA Leclerc C., Bentley S.D., Stinear T.P., Brisse S., Medigue C., Parkhill J.,
RA Cruveiller S., Brosch R.;
RT "Genomic analysis of smooth tubercle bacilli provides insights into
RT ancestry and pathoadaptation of Mycobacterium tuberculosis.";
RL Nat. Genet. 45:172-179(2013).
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; HE572590; CCC44603.1; -; Genomic_DNA.
DR AlphaFoldDB; G0TNF0; -.
DR KEGG; mce:MCAN_22711; -.
DR HOGENOM; CLU_015740_5_1_11; -.
DR OMA; GVMTIMN; -.
DR Proteomes; UP000008896; 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; 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:SF35; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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 Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 28..386
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 411..505
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 516 AA; 54220 MW; E34BF6135F1C5D77 CRC64;
MLMPHSAALN AARRSADLTA LADGGALDVI VIGGGITGVG IALDAATRGL TVALVEKHDL
AFGTSRWSSK LVHGGLRYLA SGNVGIARRS AVERGILMTR NAPHLVHAMP QLVPLLPSMG
HTKRALVRAG FLAGDALRVL AGTPAATLPR SRRIPASRVV EIAPTVRRDG LDGGLLAYDG
QLIDDARLVM AVARTAAQHG ARILTYVGAS NVTGTSVELT DRRTRQSFAL SARAVINAAG
VWAGEIDPSL TLRPSRGTHL VFDAKSFANP TAALTIPIPG ELNRFVFAMP EQLGRIYLGL
TDEDAPGPIP DVPQPSSEEI TFLLDTVNTA LGTAVGTKDV IGAYAGLRPL IDTGGAGVQG
RTADVSRDHA VFESPSGVIS VVGGKLTEYR YMAEDVLNRA ITLRHLRAAK CRTRNLPLIG
APANPGPAPG SGARLPESLV ARYGAEAANV AAAATCERPT EPVADGIDVT RAEFEYAVTH
EGALDVDDIL DRRTRIGLVP RDRERVVAVA KEFLSR
//