ProGT12.1 (Ppm1)

Home -> ProGTdb -> Search ProGT_Accessory -> Display data

ProGT ID ProGT12.1 (Ppm1)
Organism Information
Organism NameMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Domain Bacteria
Classification Phylum : Actinobacteria
Class : Actinomycetia
Orders : Corynebacteriales
Family : Mycobacteriaceae
Genus : Mycobacterium
Species : tuberculosis
Strain : H37Rv
Taxonomic ID (NCBI)83332
Genome Information
Gene BankAL123456.3
EMBLAL123456.3
Gene Information
Gene Nameppm1 
NCBI Gene ID887402
NCBI Reference SequenceNC_000962.3.
Protein information
Protein NamePpm1 
UniProtKB/ SwissProt IDO53493
NCBI Ref SeqWP_003902238.1.
UniProtKB Sequence>sp|O53493|PPMNT_MYCTU Bifunctional apolipoprotein N-acyltransferase/polyprenol monophosphomannose synthase OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=ppm1 PE=1 SV=1 MKLGAWVAAQLPTTRTAVRTRLTRLVVSIVAGLLLYASFPPRNCWWAAVVALALLAWVLT HRATTPVGGLGYGLLFGLVFYVSLLPWIGELVGPGPWLALATTCALFPGIFGLFAVVVRL LPGWPIWFAVGWAAQEWLKSILPFGGFPWGSVAFGQAEGPLLPLVQLGGVALLSTGVALV GCGLTAIALEIEKWWRTGGQGDAPPAVVLPAACICLVLFAAIVVWPQVRHAGSGSGGEPT VTVAVVQGNVPRLGLDFNAQRRAVLDNHVEETLRLAADVHAGLAQQPQFVIWPENSSDID PFVNPDAGQRISAAAEAIGAPILIGTLMDVPGRPRENPEWTNTAIVWNPGTGPADRHDKA IVQPFGEYLPMPWLFRHLSGYADRAGHFVPGNGTGVVRIAGVPVGVATCWEVIFDRAPRK SILGGAQLLTVPSNNATFNKTMSEQQLAFAKVRAVEHDRYVVVAGTTGISAVIAPDGGEL IRTDFFQPAYLDSQVRLKTRLTPATRWGPILQWILVGAAAAVVLVAMRQNGWFPRPRRSE PKGENDDSDAPPGRSEASGPPALSESDDELIQPEQGGRHSSGFGRHRATSRSYMTTGQPA PPAPGNRPSQRVLVIIPTFNERENLPVIHRRLTQACPAVHVLVVDDSSPDGTGQLADELA QADPGRTHVMHRTAKNGLGAAYLAGFAWGLSREYSVLVEMDADGSHAPEQLQRLLDAVDA GADLAIGSRYVAGGTVRNWPWRRLVLSKTANTYSRLALGIGIHDITAGYRAYRREALEAI DLDGVDSKGYCFQIDLTWRTVSNGFVVTEVPITFTERELGVSKMSGSNIREALVKVARWG IEGRLSRSDHARARPDIARPGAGGSRVSRADVTE
EMBL CDSCCP44824.1.
Sequence length874 AA
Subcellular LocationMembrane (Integral component of membrane)
String83332.Rv2051c.
Glycosylation Information
CAZY FamilyGT2
EC Number (BRENDA)2.4.1.-
Sugar Donor SpecificityGDP-Mannose 
Acceptor Substrate SpecificityDolichyl phosphate
ProductDolichyl D-mannosyl phosphate
Donor SpecificityGDP-Mannose
Function in Glycosylation pathway1) Transfer mannose to endogenous polyprenol phosphate.
Additional Information1) M. tuberculosis Ppm is able to complement Streptomyces coelicolor Ppm and Lnt1 (Lipoprotein N-acyl transferase) mutant strain for glycosylation of protein. 
Litrature
Year Of Validation2002 
Reference Gurcha, S.S., Baulard, A.R., Kremer, L., Locht, C., Moody, D.B., Muhlecker, W., Costello, C.E., Crick, D.C., Brennan, P.J. and Besra, G.S., 2002. Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium tuberculosis. Biochemical Journal, 365(2), pp.441-450.

Corresponding AuthorSchool of Biosciences, The University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Reference Gurcha, S.S., Baulard, A.R., Kremer, L., Locht, C., Moody, D.B., Muhlecker, W., Costello, C.E., Crick, D.C., Brennan, P.J. and Besra, G.S., 2002. Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium tuberculosis. Biochemical Journal, 365(2), pp.441-450.

Corresponding AuthorSchool of Biosciences, The University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Reference Liu, C.F., Tonini, L., Malaga, W., Beau, M., Stella, A., Bouyssié, D., Jackson, M.C., Nigou, J., Puzo, G., Guilhot, C. and Burlet-Schiltz, O., 2013. Bacterial protein-O-mannosylating enzyme is crucial for virulence of Mycobacterium tuberculosis. Proceedings of the National Academy of Sciences, 110(16), pp.6560-6565.

Corresponding Author1.National Center for Scientific Research, Institute of Pharmacology and Structural Biology, F-31077 Toulouse, Franceb. 2. University of Toulouse, Paul Sabatier University, Institute of Pharmacology and Structural Biology
Reference Córdova-Dávalos, L.E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G. and Servín-González, L., 2014. Lipoprotein N-acyl transferase (Lnt1) is dispensable for protein O-mannosylation by Streptomyces coelicolor. FEMS microbiology letters, 350(1), pp.72-82.

Corresponding AuthorDepartment of Molecular Biology and Biotechnology, Institute of Biomedical Research, National Autonomous University of Mexico, Ciudad University, Mexico City, Mexico City.