GLFT1_MYCTU
ID GLFT1_MYCTU Reviewed; 304 AA.
AC P9WMX3; L0TGJ5; Q79F98; Q7D4V6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Galactofuranosyltransferase GlfT1 {ECO:0000305};
DE Short=GalTr 1 {ECO:0000305};
DE EC=2.4.1.287 {ECO:0000269|PubMed:16952951};
DE AltName: Full=Arabinogalactan galactosyltransferase 1 {ECO:0000305};
DE AltName: Full=Rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,4/1,5-galactofuranosyltransferase;
DE AltName: Full=UDP-Galf:alpha-3-L-rhamnosyl-alpha-D-GlcNAc-pyrophosphate polyprenol, galactofuranosyl transferase;
GN Name=glfT1 {ECO:0000312|EMBL:CCP46611.1}; OrderedLocusNames=Rv3782;
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., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=H37Rv;
RX PubMed=16952951; DOI=10.1128/jb.00489-06;
RA Mikusova K., Belanova M., Kordulakova J., Honda K., McNeil M.R.,
RA Mahapatra S., Crick D.C., Brennan P.J.;
RT "Identification of a novel galactosyl transferase involved in biosynthesis
RT of the mycobacterial cell wall.";
RL J. Bacteriol. 188:6592-6598(2006).
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 tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=H37Rv;
RX PubMed=18248822; DOI=10.1016/j.pep.2007.11.012;
RA Alderwick L.J., Dover L.G., Veerapen N., Gurcha S.S., Kremer L.,
RA Roper D.L., Pathak A.K., Reynolds R.C., Besra G.S.;
RT "Expression, purification and characterisation of soluble GlfT and the
RT identification of a novel galactofuranosyltransferase Rv3782 involved in
RT priming GlfT-mediated galactan polymerisation in Mycobacterium
RT tuberculosis.";
RL Protein Expr. Purif. 58:332-341(2008).
RN [5]
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., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP INTERACTION WITH RV3789.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23038254; DOI=10.1074/jbc.m112.400986;
RA Larrouy-Maumus G., Skovierova H., Dhouib R., Angala S.K., Zuberogoitia S.,
RA Pham H., Villela A.D., Mikusova K., Noguera A., Gilleron M.,
RA Valentinova L., Kordulakova J., Brennan P.J., Puzo G., Nigou J.,
RA Jackson M.;
RT "A small multidrug resistance-like transporter involved in the
RT arabinosylation of arabinogalactan and lipoarabinomannan in mycobacteria.";
RL J. Biol. Chem. 287:39933-39941(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG)
CC region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC essential component of the mycobacterial cell wall. Catalyzes the
CC transfer of the first two galactofuranosyl (Galf) units from UDP-
CC galactofuranose (UDP-Galf) onto the rhamnosyl-GlcNAc-diphospho-
CC decaprenol (Rha-GlcNAc-PP-C50) acceptor, yielding galactofuranosyl-
CC galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-
CC GlcNAc-PP-C50). Thus, GlfT1 is the initiator of galactan synthesis,
CC while GlfT2 continues with the subsequent polymerization events.
CC {ECO:0000269|PubMed:16952951}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-
CC diphospho-trans,octa-cis-decaprenol + 2 UDP-alpha-D-galactofuranose =
CC beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-
CC L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC trans,octa-cis-decaprenol + 2 H(+) + 2 UDP; Xref=Rhea:RHEA:34379,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66915,
CC ChEBI:CHEBI:67209, ChEBI:CHEBI:67210; EC=2.4.1.287;
CC Evidence={ECO:0000269|PubMed:16952951};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 mM for O-decenyl beta-D-Galf(1->6)-beta-D-Galf (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18248822};
CC KM=3.77 mM for O-decenyl beta-D-Galf(1->5)-beta-D-Galf (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18248822};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:16952951}.
CC -!- SUBUNIT: Interacts with Rv3789. Is thus probably part of an AG
CC biosynthetic complex. {ECO:0000269|PubMed:23038254}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16952951}.
CC Secreted, cell wall {ECO:0000269|PubMed:16952951}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000305|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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; AL123456; CCP46611.1; -; Genomic_DNA.
DR PIR; B70696; B70696.
DR RefSeq; WP_003420606.1; NZ_NVQJ01000009.1.
DR RefSeq; YP_178014.1; NC_000962.3.
DR AlphaFoldDB; P9WMX3; -.
DR SMR; P9WMX3; -.
DR STRING; 83332.Rv3782; -.
DR PaxDb; P9WMX3; -.
DR DNASU; 886114; -.
DR GeneID; 886114; -.
DR KEGG; mtu:Rv3782; -.
DR TubercuList; Rv3782; -.
DR eggNOG; COG1216; Bacteria.
DR OMA; RFYTYRN; -.
DR PhylomeDB; P9WMX3; -.
DR BioCyc; MetaCyc:G185E-8078-MON; -.
DR BRENDA; 2.4.1.287; 3445.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IDA:UniProtKB.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Membrane; Reference proteome; Secreted; Transferase.
FT CHAIN 1..304
FT /note="Galactofuranosyltransferase GlfT1"
FT /id="PRO_0000395355"
SQ SEQUENCE 304 AA; 33864 MW; 66AC155D0370FFCA CRC64;
MTESVFAVVV THRRPDELAK SLDVLTAQTR LPDHLIVVDN DGCGDSPVRE LVAGQPIATT
YLGSRRNLGG AGGFALGMLH ALAQGADWVW LADDDGHAQD ARVLATLLAC AEKYSLAEVS
PMVCNIDDPT RLAFPLRRGL VWRRRASELR TEAGQELLPG IASLFNGALF RASTLAAIGV
PDLRLFIRGD EVEMHRRLIR SGLPFGTCLD AAYLHPCGSD EFKPILCGRM HAQYPDDPGK
RFFTYRNRGY VLSQPGLRKL LAQEWLRFGW FFLVTRRDPK GLWEWIRLRR LGRREKFGKP
GGSA
