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Protein

Galactofuranosyl transferase GlfT2

Gene

glfT2

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the polymerization of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component the mycobacteria cell wall, through successively beta-D-(1->5) and beta-D-(1->6)-galactofuranosyltransferases activities. It transfers the galactofuranosyl (Galf) unit from UDP-galactofuranosyl (UDP-Galf) onto the galactofuranosyl-rhamnosyl-GlcNAc-pyrophosphoryl-undecaprenyl (Galf-Rha-GlcNAc-PP-C55), yielding polygalactofuranosyl-rhamnosyl-GlcNAc-pyrophosphoryl-undecaprenyl ((Galf)x-Rha-GlcNAc-PP-C55). It is able to transfer Galf onto beta-D-(1->5) or beta-D-(1->6) linked acceptor, but has a stronger affinity for beta-D-(1->6) acceptor.6 Publications

Catalytic activityi

28 UDP-alpha-D-galactofuranose + beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol = 28 UDP + (beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6))(14)-beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-trans,octacis-decaprenol.2 Publications

Cofactori

Mn2+1 Publication, Mg2+1 Publication

Kineticsi

  1. KM=0.38 mM for UDP-Galf3 Publications
  2. KM=0.38 mM for UDP-Galf (at pH 7.9)3 Publications
  1. Vmax=4.4 µmol/min/mg enzyme3 Publications

Pathwayi: cell wall polysaccharide biosynthesis

This protein is involved in the pathway cell wall polysaccharide biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway cell wall polysaccharide biosynthesis and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711Substrate1 Publication
Binding sitei200 – 2001Substrate1 Publication
Binding sitei229 – 2291Substrate1 Publication
Metal bindingi256 – 2561Manganese
Binding sitei256 – 2561Substrate1 Publication
Metal bindingi258 – 2581Manganese
Active sitei272 – 2721Proton acceptorCurated
Metal bindingi396 – 3961Manganese

GO - Molecular functioni

  • lipopolysaccharide-1,5-galactosyltransferase activity Source: MTBBASE
  • lipopolysaccharide-1,6-galactosyltransferase activity Source: MTBBASE
  • metal ion binding Source: UniProtKB-KW
  • transferase activity Source: UniProtKB
  • transferase activity, transferring glycosyl groups Source: UniProtKB
  • UDP-galactosyltransferase activity Source: MTBBASE

GO - Biological processi

  • capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
  • cell wall macromolecule biosynthetic process Source: UniProtKB
  • cell wall organization Source: UniProtKB
  • cell wall polysaccharide biosynthetic process Source: MTBBASE
  • growth Source: MTBBASE
  • lipopolysaccharide biosynthetic process Source: MTBBASE
  • mycolate cell wall layer assembly Source: MTBBASE
  • UDP-D-galactose metabolic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15256.
MTBRV:RV3808C-MONOMER.
BRENDAi2.4.1.288. 3445.
UniPathwayiUPA00963.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Galactofuranosyl transferase GlfT2 (EC:2.4.1.288)
Short name:
GalTr
Alternative name(s):
Beta-D-(1->5)galactofuranosyltransferase
Beta-D-(1->6)galactofuranosyltransferase
Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase
UDP-Galf:alpha-3-L-rhamnosyl-alpha-D-GlcNAc-pyrophosphate polyprenol, UDP-galactofuranosyl transferase
Gene namesi
Name:glfT2
Ordered Locus Names:Rv3808c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3808c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi300 – 3001E → S: Almost identical transferase activity than wild-type. 1 Publication
Mutagenesisi371 – 3711D → S: Loss of transferase activity. 1 Publication
Mutagenesisi372 – 3721D → S: Loss of transferase activity. 1 Publication
Mutagenesisi399 – 3991W → S: Almost identical transferase activity than wild-type. 1 Publication
Mutagenesisi413 – 4131H → S: Almost identical transferase activity than wild-type. 1 Publication

Chemistry

ChEMBLiCHEMBL1075096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Galactofuranosyl transferase GlfT2PRO_0000395356Add
BLAST

Proteomic databases

PaxDbiO53585.
PRIDEiO53585.

Interactioni

Subunit structurei

Dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3808c.

Chemistry

BindingDBiO53585.

Structurei

Secondary structure

1
637
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 75Combined sources
Beta strandi8 – 114Combined sources
Helixi21 – 244Combined sources
Turni25 – 273Combined sources
Beta strandi34 – 363Combined sources
Beta strandi39 – 424Combined sources
Beta strandi45 – 484Combined sources
Beta strandi53 – 553Combined sources
Turni59 – 613Combined sources
Helixi65 – 717Combined sources
Beta strandi75 – 9420Combined sources
Beta strandi100 – 11011Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi128 – 1303Combined sources
Beta strandi133 – 1419Combined sources
Beta strandi143 – 1519Combined sources
Beta strandi162 – 1654Combined sources
Beta strandi168 – 1703Combined sources
Helixi172 – 18211Combined sources
Helixi186 – 1894Combined sources
Beta strandi192 – 1998Combined sources
Beta strandi201 – 2033Combined sources
Helixi205 – 2073Combined sources
Helixi211 – 2188Combined sources
Helixi219 – 2213Combined sources
Beta strandi222 – 2265Combined sources
Helixi231 – 24616Combined sources
Beta strandi250 – 2556Combined sources
Beta strandi257 – 2615Combined sources
Helixi264 – 27512Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi281 – 2888Combined sources
Beta strandi300 – 3034Combined sources
Turni304 – 3074Combined sources
Beta strandi308 – 3114Combined sources
Turni321 – 3233Combined sources
Helixi331 – 3344Combined sources
Helixi335 – 3373Combined sources
Beta strandi349 – 3535Combined sources
Helixi354 – 3607Combined sources
Beta strandi367 – 3704Combined sources
Helixi371 – 38111Combined sources
Beta strandi386 – 39611Combined sources
Beta strandi399 – 4024Combined sources
Beta strandi405 – 4073Combined sources
Helixi409 – 42416Combined sources
Helixi429 – 4313Combined sources
Helixi432 – 44817Combined sources
Helixi452 – 46615Combined sources
Helixi469 – 4746Combined sources
Turni475 – 4784Combined sources
Helixi479 – 4879Combined sources
Helixi491 – 4933Combined sources
Beta strandi494 – 4974Combined sources
Helixi499 – 5013Combined sources
Helixi518 – 53215Combined sources
Helixi538 – 5414Combined sources
Beta strandi545 – 5484Combined sources
Helixi550 – 5523Combined sources
Helixi555 – 5584Combined sources
Beta strandi562 – 5676Combined sources
Beta strandi574 – 5785Combined sources
Helixi581 – 61131Combined sources
Helixi613 – 6175Combined sources
Helixi619 – 6268Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FIXX-ray2.45A/B1-637[»]
4FIYX-ray3.10A/B1-637[»]
ProteinModelPortaliO53585.
SMRiO53585. Positions 1-629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiENOG410602S. Bacteria.
COG1216. LUCA.
HOGENOMiHOG000247585.
KOiK16650.
OMAiDVDFNGW.
PhylomeDBiO53585.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

O53585-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELAASLLS RVILPRPGEP LDVRKLYLEE STTNARRAHA PTRTSLQIGA
60 70 80 90 100
ESEVSFATYF NAFPASYWRR WTTCKSVVLR VQVTGAGRVD VYRTKATGAR
110 120 130 140 150
IFVEGHDFTG TEDQPAAVET EVVLQPFEDG GWVWFDITTD TAVTLHSGGW
160 170 180 190 200
YATSPAPGTA NIAVGIPTFN RPADCVNALR ELTADPLVDQ VIGAVIVPDQ
210 220 230 240 250
GERKVRDHPD FPAAAARLGS RLSIHDQPNL GGSGGYSRVM YEALKNTDCQ
260 270 280 290 300
QILFMDDDIR LEPDSILRVL AMHRFAKAPM LVGGQMLNLQ EPSHLHIMGE
310 320 330 340 350
VVDRSIFMWT AAPHAEYDHD FAEYPLNDNN SRSKLLHRRI DVDYNGWWTC
360 370 380 390 400
MIPRQVAEEL GQPLPLFIKW DDADYGLRAA EHGYPTVTLP GAAIWHMAWS
410 420 430 440 450
DKDDAIDWQA YFHLRNRLVV AAMHWDGPKA QVIGLVRSHL KATLKHLACL
460 470 480 490 500
EYSTVAIQNK AIDDFLAGPE HIFSILESAL PQVHRIRKSY PDAVVLPAAS
510 520 530 540 550
ELPPPLHKNK AMKPPVNPLV IGYRLARGIM HNLTAANPQH HRRPEFNVPT
560 570 580 590 600
QDARWFLLCT VDGATVTTAD GCGVVYRQRD RAKMFALLWQ SLRRQRQLLK
610 620 630
RFEEMRRIYR DALPTLSSKQ KWETALLPAA NQEPEHG
Length:637
Mass (Da):71,507
Last modified:June 1, 1998 - v1
Checksum:iD7C9AB28B5005B66
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46637.1.
PIRiD70888.
RefSeqiNP_218325.1. NC_000962.3.
WP_003900761.1. NZ_KK339374.1.

Genome annotation databases

EnsemblBacteriaiCCP46637; CCP46637; Rv3808c.
GeneIDi886136.
KEGGimtu:Rv3808c.
PATRICi18157074. VBIMycTub87468_4239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46637.1.
PIRiD70888.
RefSeqiNP_218325.1. NC_000962.3.
WP_003900761.1. NZ_KK339374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FIXX-ray2.45A/B1-637[»]
4FIYX-ray3.10A/B1-637[»]
ProteinModelPortaliO53585.
SMRiO53585. Positions 1-629.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3808c.

Chemistry

BindingDBiO53585.
ChEMBLiCHEMBL1075096.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbiO53585.
PRIDEiO53585.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46637; CCP46637; Rv3808c.
GeneIDi886136.
KEGGimtu:Rv3808c.
PATRICi18157074. VBIMycTub87468_4239.

Organism-specific databases

TubercuListiRv3808c.

Phylogenomic databases

eggNOGiENOG410602S. Bacteria.
COG1216. LUCA.
HOGENOMiHOG000247585.
KOiK16650.
OMAiDVDFNGW.
PhylomeDBiO53585.

Enzyme and pathway databases

UniPathwayiUPA00963.
BioCyciMetaCyc:MONOMER-15256.
MTBRV:RV3808C-MONOMER.
BRENDAi2.4.1.288. 3445.

Miscellaneous databases

PROiO53585.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiGLFT2_MYCTU
AccessioniPrimary (citable) accession number: O53585
Secondary accession number(s): L0TFB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.