Latest update: September 24, 2018


ProGT12.1 (Ppm1)

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ProGT ID ProGT12.1 (Ppm1)
Organism Information
Organism NameMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Domain Bacteria
PhylumActinobacteria
ClassificationFamily: Mycobacteriaceae
Suborder: Corynebacterineae
Order: Actinomycetales
Subclass: Actinobacteridae
Class: Actinobacteria
Division or phylum: "Actinobacteria"
Taxonomic ID (NCBI)83332
Genome Information
Gene BankAL123456
EMBLAL123456
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. & Besra, G. S. (2002). Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium tuberculosis. Biochemical Journal, 365(2), 441-450.

Authors Gurcha, S.S., Baulard, A.R., Kremer, L., Locht, C., Moody, D.B., Muhlecker, W., Costello, C.E., Crick, D.C., Brennan, P.J. & Besra, G. S.
Research groupsDepartment of Microbiology and Immunology, The Medical School, The University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, UK.
Corresponding Author Besra, G. S.
ContactsDepartment of Microbiology and Immunology, The Medical School, The University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, UK.
Reference Liu, C.F., Tonini, L., Malaga, W., Beau, M., Stella, A., Bouyssié, D., Jackson, M.C., Nigou, J., Puzo, G., Guilhot, C. & Burlet-Schiltz, O. (2013). Bacterial protein-O-mannosylating enzyme is crucial for virulence of Mycobacterium tuberculosis. Proceedings of the National Academy of Sciences, 201219704.

Authors Liu, C.F., Tonini, L., Malaga, W., Beau, M., Stella, A., Bouyssié, D., Jackson, M.C., Nigou, J., Puzo, G., Guilhot, C. & Burlet-Schiltz, O.
Research groupsScientific Research National Center, Institute of Pharmacology and Structural Biology, F-31077 Toulouse, France.
Corresponding Author Besra, G. S.
ContactsScientific Research National Center, Institute of Pharmacology and Structural Biology, F-31077 Toulouse, France.
Reference Córdova-Dávalos, L. E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G., & Servín-González, L. (2014). Lipoprotein N-acyl transferase (Lnt1) is dispensable for protein O-mannosylation by Streptomyces coelicolor. FEMS microbiology letters, 350(1), 72-82.

Authors Córdova-Dávalos, L. E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G., & Servín-González, L.
Research groupsDepartment of Molecular Biology and Biotechnology, Institute of Biomedical Research, National Autonomous University of Mexico, Ciudad Universitaria, Mexico City, Mexico City.
Corresponding Author Servín-González, L.
ContactsScientific Research National Center, Institute of Pharmacology and Structural Biology, F-31077 Toulouse, France.
Reference Córdova-Dávalos, L. E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G., & Servín-González, L. (2014). Lipoprotein N-acyl transferase (Lnt1) is dispensable for protein O-mannosylation by Streptomyces coelicolor. FEMS microbiology letters, 350(1), 72-82.

Authors Córdova-Dávalos, L. E., Espitia, C., González-Cerón, G., Arreguín-Espinosa, R., Soberón-Chávez, G., & Servín-González, L
Research groupsDepartment of Molecular Biology and Biotechnology, Institute of Biomedical Research, National Autonomous University of Mexico, Ciudad University, Mexico City, Mexico City.
Corresponding Author Servín-González, L
ContactsDepartment of Molecular Biology and Biotechnology, Institute of Biomedical Research, National Autonomous University of Mexico, Ciudad University, Mexico City, Mexico City.