ID GLFT2_MYCTU Reviewed; 637 AA. AC O53585; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 19-OCT-2011, entry version 49. DE RecName: Full=UDP-galactofuranosyl transferase GlfT2; DE Short=GalTr; DE EC=2.4.1.-; DE AltName: Full=Beta-D-(1-5)galactofuranosyltransferase; DE AltName: Full=Beta-D-(1-6)galactofuranosyltransferase; DE AltName: Full=UDP-Galf:alpha-3-L-rhamnosyl-alpha-D-GlcNAc-pyrophosphate polyprenol, UDP-galactofuranosyl transferase; GN Name=glfT2; OrderedLocusNames=Rv3808c; OS Mycobacterium tuberculosis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=1773; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX MEDLINE=98295987; 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 FUNCTION AS A UDP-GALACTOFURANOSYLTRANSFERASE, AND NOMENCLATURE. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=11304545; DOI=10.1074/jbc.M102022200; RA Kremer L., Dover L.G., Morehouse C., Hitchin P., Everett M., RA Morris H.R., Dell A., Brennan P.J., McNeil M.R., Flaherty C., RA Duncan K., Besra G.S.; RT "Galactan biosynthesis in Mycobacterium tuberculosis. Identification RT of a bifunctional UDP-galactofuranosyltransferase."; RL J. Biol. Chem. 276:26430-26440(2001). RN [3] RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS]. RX PubMed=19099550; DOI=10.1186/1752-0509-2-109; RA Raman K., Yeturu K., Chandra N.; RT "targetTB: a target identification pipeline for Mycobacterium RT tuberculosis through an interactome, reactome and genome-scale RT structural analysis."; RL BMC Syst. Biol. 2:109-109(2008). RN [4] RP SUBSTRATE SPECIFICITY. RX PubMed=18055597; DOI=10.1128/JB.01326-07; RA Belanova M., Dianiskova P., Brennan P.J., Completo G.C., Rose N.L., RA Lowary T.L., Mikusova K.; RT "Galactosyl transferases in mycobacterial cell wall synthesis."; RL J. Bacteriol. 190:1141-1145(2008). CC -!- FUNCTION: Involved in the polymerization of the arabinogalactan CC (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) CC complex, an essential component the mycobacteria cell wall, CC through successively beta-D-(1->5) and beta-D-(1->6)- CC galactofuranosyltransferases activities. It transfers the CC galactofuranosyl (Galf) unit from UDP-galactofuranosyl (UDP-Galf) CC onto the galactofuranosyl-rhamnosyl-GlcNAc-pyrophosphoryl- CC undecaprenyl (Galf-Rha-GlcNAc-PP-C55), yielding CC polygalactofuranosyl-rhamnosyl-GlcNAc-pyrophosphoryl-undecaprenyl CC ((Galf)x-Rha-GlcNAc-PP-C55). It is able to transfer Galf onto CC beta-D-(1->5) or beta-D-(1->6) linked acceptor, but has a stronger CC affinity for beta-D-(1->6) acceptor. CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX842584; CAA17872.1; -; Genomic_DNA. DR PIR; D70888; D70888. DR RefSeq; NP_218325.1; NC_000962.2. DR ProteinModelPortal; O53585; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; EBMYCT00000003922; EBMYCP00000003922; EBMYCG00000003920. DR GeneID; 886136; -. DR GenomeReviews; AL123456_GR; Rv3808c. DR KEGG; mtu:Rv3808c; -. DR TubercuList; Rv3808c; -. DR GeneTree; EBGT00050000017089; -. DR HOGENOM; HBG657765; -. DR OMA; LCLEYST; -. DR ProtClustDB; CLSK872249; -. DR BioCyc; MetaCyc:MONOMER-15256; -. DR GO; GO:0005829; C:cytosol; IDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; IDA:MTBBASE. DR GO; GO:0035496; F:lipopolysaccharide-1,5-galactosyltransferase activity; IDA:MTBBASE. DR GO; GO:0008921; F:lipopolysaccharide-1,6-galactosyltransferase activity; IDA:MTBBASE. DR GO; GO:0070592; P:cell wall polysaccharide biosynthetic process; IDA:MTBBASE. DR GO; GO:0007047; P:cellular cell wall organization; IDA:UniProtKB. DR GO; GO:0040007; P:growth; IMP:MTBBASE. DR GO; GO:0071769; P:mycolate cell wall layer assembly; IDA:MTBBASE. PE 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 637 UDP-galactofuranosyl transferase GlfT2. FT /FTId=PRO_0000395356. SQ SEQUENCE 637 AA; 71507 MW; D7C9AB28B5005B66 CRC64; MSELAASLLS RVILPRPGEP LDVRKLYLEE STTNARRAHA PTRTSLQIGA ESEVSFATYF NAFPASYWRR WTTCKSVVLR VQVTGAGRVD VYRTKATGAR IFVEGHDFTG TEDQPAAVET EVVLQPFEDG GWVWFDITTD TAVTLHSGGW YATSPAPGTA NIAVGIPTFN RPADCVNALR ELTADPLVDQ VIGAVIVPDQ GERKVRDHPD FPAAAARLGS RLSIHDQPNL GGSGGYSRVM YEALKNTDCQ QILFMDDDIR LEPDSILRVL AMHRFAKAPM LVGGQMLNLQ EPSHLHIMGE VVDRSIFMWT AAPHAEYDHD FAEYPLNDNN SRSKLLHRRI DVDYNGWWTC MIPRQVAEEL GQPLPLFIKW DDADYGLRAA EHGYPTVTLP GAAIWHMAWS DKDDAIDWQA YFHLRNRLVV AAMHWDGPKA QVIGLVRSHL KATLKHLACL EYSTVAIQNK AIDDFLAGPE HIFSILESAL PQVHRIRKSY PDAVVLPAAS ELPPPLHKNK AMKPPVNPLV IGYRLARGIM HNLTAANPQH HRRPEFNVPT QDARWFLLCT VDGATVTTAD GCGVVYRQRD RAKMFALLWQ SLRRQRQLLK RFEEMRRIYR DALPTLSSKQ KWETALLPAA NQEPEHG //