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Database: UniProt
Entry: P9WN79
LinkDB: P9WN79
Original site: P9WN79 
ID   GLPD2_MYCTU             Reviewed;         585 AA.
AC   P9WN79; L0TDR3; O07168; P64184;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   13-FEB-2019, entry version 28.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 2;
DE            EC=1.1.5.3;
GN   Name=glpD2; OrderedLocusNames=Rv3302c;
GN   ORFNames=MTCI418A.04c, MTV016.01c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.M111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC         dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:132124; EC=1.1.5.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AL123456; CCP46121.1; -; Genomic_DNA.
DR   PIR; H70533; H70533.
DR   RefSeq; NP_217819.1; NC_000962.3.
DR   RefSeq; WP_003417217.1; NZ_NVQJ01000003.1.
DR   ProteinModelPortal; P9WN79; -.
DR   SMR; P9WN79; -.
DR   STRING; 83332.Rv3302c; -.
DR   PaxDb; P9WN79; -.
DR   PRIDE; P9WN79; -.
DR   EnsemblBacteria; CCP46121; CCP46121; Rv3302c.
DR   GeneID; 887211; -.
DR   KEGG; mtu:Rv3302c; -.
DR   TubercuList; Rv3302c; -.
DR   eggNOG; ENOG4105C6V; Bacteria.
DR   eggNOG; COG0578; LUCA.
DR   KO; K00111; -.
DR   OMA; MDNPTVK; -.
DR   PhylomeDB; P9WN79; -.
DR   BioCyc; MTBH37RV:G185E-7576-MONOMER; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central.
DR   GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central.
DR   GO; GO:0052591; F:sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
DR   PROSITE; PS00978; FAD_G3PDH_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; FAD; Flavoprotein; Glycerol metabolism;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    585       Glycerol-3-phosphate dehydrogenase 2.
FT                                /FTId=PRO_0000126102.
FT   NP_BIND      37     65       FAD. {ECO:0000250}.
SQ   SEQUENCE   585 AA;  62778 MW;  760C15F7E75BB69F CRC64;
     MSNPIQAPDG GQGWPAAALG PAQRAVAWKR LGTEQFDVVV IGGGVVGSGC ALDAATRGLK
     VALVEARDLA SGTSSRSSKM FHGGLRYLEQ LEFGLVREAL YERELSLTTL APHLVKPLPF
     LFPLTKRWWE RPYIAAGIFL YDRLGGAKSV PAQRHFTRAG ALRLSPGLKR SSLIGGIRYY
     DTVVDDARHT MTVARTAAHY GAVVRCSTQV VALLREGDRV IGVGVRDSEN GAVAEVRGHV
     VVNATGVWTD EIQALSKQRG RFQVRASKGV HVVVPRDRIV SDVAMILRTE KSVMFVIPWG
     SHWIIGTTDT DWNLDLAHPA ATKADIDYIL GTVNAVLATP LTHADIDGVY AGLRPLLAGE
     SDDTSKLSRE HAVAVPAAGL VAIAGGKYTT YRVMAADAID AAVQFIPARV APSITEKVSL
     LGADGYFALV NQAEHVGALQ GLHPYRVRHL LDRYGSLISD VLAMAASDPS LLSPITEAPG
     YLKVEAAYAA AAEGALHLED ILARRMRISI EYPHRGVDCA REVAEVVAPV LGWTAADIDR
     EVANYMARVE AEVLSQAQPD DVSADMLRAS APEARAEILE PVPLD
//
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