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Database: UniProt/TrEMBL
Entry: G0TNF0_MYCCP
LinkDB: G0TNF0_MYCCP
Original site: G0TNF0_MYCCP 
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
//
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