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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)DescriptionActionsGraphical viewLength
Binding sitei171Substrate1 Publication1
Binding sitei200Substrate1 Publication1
Binding sitei229Substrate1 Publication1
Metal bindingi256Manganese1
Binding sitei256Substrate1 Publication1
Metal bindingi258Manganese1
Active sitei272Proton acceptorCurated1
Metal bindingi396Manganese1

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:G185E-8104-MONOMER.
MTBH37RV:G185E-8104-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)DescriptionActionsGraphical viewLength
Mutagenesisi300E → S: Almost identical transferase activity than wild-type. 1 Publication1
Mutagenesisi371D → S: Loss of transferase activity. 1 Publication1
Mutagenesisi372D → S: Loss of transferase activity. 1 Publication1
Mutagenesisi399W → S: Almost identical transferase activity than wild-type. 1 Publication1
Mutagenesisi413H → S: Almost identical transferase activity than wild-type. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003953561 – 637Galactofuranosyl transferase GlfT2Add BLAST637

Proteomic databases

PaxDbiO53585.

Interactioni

Subunit structurei

Dimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3808c.

Chemistry databases

BindingDBiO53585.

Structurei

Secondary structure

1637
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 7Combined sources5
Beta strandi8 – 11Combined sources4
Helixi21 – 24Combined sources4
Turni25 – 27Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi45 – 48Combined sources4
Beta strandi53 – 55Combined sources3
Turni59 – 61Combined sources3
Helixi65 – 71Combined sources7
Beta strandi75 – 94Combined sources20
Beta strandi100 – 110Combined sources11
Beta strandi112 – 114Combined sources3
Beta strandi116 – 124Combined sources9
Beta strandi128 – 130Combined sources3
Beta strandi133 – 141Combined sources9
Beta strandi143 – 151Combined sources9
Beta strandi162 – 165Combined sources4
Beta strandi168 – 170Combined sources3
Helixi172 – 182Combined sources11
Helixi186 – 189Combined sources4
Beta strandi192 – 199Combined sources8
Beta strandi201 – 203Combined sources3
Helixi205 – 207Combined sources3
Helixi211 – 218Combined sources8
Helixi219 – 221Combined sources3
Beta strandi222 – 226Combined sources5
Helixi231 – 246Combined sources16
Beta strandi250 – 255Combined sources6
Beta strandi257 – 261Combined sources5
Helixi264 – 275Combined sources12
Beta strandi276 – 278Combined sources3
Beta strandi281 – 288Combined sources8
Beta strandi300 – 303Combined sources4
Turni304 – 307Combined sources4
Beta strandi308 – 311Combined sources4
Turni321 – 323Combined sources3
Helixi331 – 334Combined sources4
Helixi335 – 337Combined sources3
Beta strandi349 – 353Combined sources5
Helixi354 – 360Combined sources7
Beta strandi367 – 370Combined sources4
Helixi371 – 381Combined sources11
Beta strandi386 – 396Combined sources11
Beta strandi399 – 402Combined sources4
Beta strandi405 – 407Combined sources3
Helixi409 – 424Combined sources16
Helixi429 – 431Combined sources3
Helixi432 – 448Combined sources17
Helixi452 – 466Combined sources15
Helixi469 – 474Combined sources6
Turni475 – 478Combined sources4
Helixi479 – 487Combined sources9
Helixi491 – 493Combined sources3
Beta strandi494 – 497Combined sources4
Helixi499 – 501Combined sources3
Helixi518 – 532Combined sources15
Helixi538 – 541Combined sources4
Beta strandi545 – 548Combined sources4
Helixi550 – 552Combined sources3
Helixi555 – 558Combined sources4
Beta strandi562 – 567Combined sources6
Beta strandi574 – 578Combined sources5
Helixi581 – 611Combined sources31
Helixi613 – 617Combined sources5
Helixi619 – 626Combined sources8

3D structure databases

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

Protein-protein interaction databases

STRINGi83332.Rv3808c.

Chemistry databases

BindingDBiO53585.
ChEMBLiCHEMBL1075096.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbiO53585.

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:G185E-8104-MONOMER.
MTBH37RV:G185E-8104-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: November 2, 2016
This is version 87 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.