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Protein

Bifunctional protein GlmU

Gene

glmU

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

Functioni

Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.UniRule annotation2 Publications

Catalytic activityi

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation2 Publications
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine.UniRule annotation2 Publications

Cofactori

Mg2+5 Publications, Co2+2 PublicationsNote: Binds 1 Mg2+ ion per subunit (PubMed:19237750, PubMed:19121323, Ref.7, Ref.8, PubMed:23485416). Can also use Co2+ ion to a lesser extent (Ref.8) (PubMed:23485416).5 Publications

Kineticsi

  1. KM=106.75 µM for GlcNAc-1-P (at pH 7.6)1 Publication
  2. KM=61.86 µM for UTP (at pH 7.6)1 Publication
  3. KM=240 µM for GlcN-1-P (at pH 7.6)1 Publication
  4. KM=304 µM for acetyl-CoA (at pH 7.6)1 Publication
  1. Vmax=1.869 µmol/min/mg enzyme (Uridyltransferase activity) (at pH 7.6)1 Publication
  2. Vmax=4.489 µmol/min/mg enzyme (Acetyltransferase activity) (at pH 7.6)1 Publication

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Bifunctional protein GlmU (glmU), Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional protein GlmU (glmU), Bifunctional protein GlmU (glmU)
This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate, the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS lipid A biosynthesis

This protein is involved in the pathway LPS lipid A biosynthesis, which is part of Bacterial outer membrane biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway LPS lipid A biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei26UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei83UDP-GlcNAcUniRule annotation2 Publications1
Metal bindingi114Magnesium or cobalt4 Publications1
Binding sitei151UDP-GlcNAc; via amide nitrogenUniRule annotation4 Publications1
Binding sitei166UDP-GlcNAcUniRule annotation4 Publications1
Binding sitei181UDP-GlcNAcUniRule annotation4 Publications1
Metal bindingi239Magnesium or cobalt4 Publications1
Binding sitei239UDP-GlcNAcUniRule annotation4 Publications1
Binding sitei344UDP-GlcNAcUniRule annotation2 Publications1
Binding sitei362UDP-GlcNAcUniRule annotation2 Publications1
Active sitei374Proton acceptorUniRule annotation1 Publication1
Binding sitei377UDP-GlcNAcUniRule annotation2 Publications1
Binding sitei388UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei391Acetyl-CoA; via amide nitrogenUniRule annotation1 Publication1
Binding sitei416Acetyl-CoA; via carbonyl oxygenUniRule annotation1 Publication1
Binding sitei434Acetyl-CoA; via amide nitrogen1 Publication1

GO - Molecular functioni

  • glucosamine-1-phosphate N-acetyltransferase activity Source: MTBBASE
  • magnesium ion binding Source: MTBBASE
  • UDP-N-acetylglucosamine diphosphorylase activity Source: MTBBASE
  • uridylyltransferase activity Source: MTBBASE

GO - Biological processi

  • adhesion of symbiont to host cell Source: AgBase
  • cell morphogenesis Source: UniProtKB-HAMAP
  • cell wall organization Source: UniProtKB-KW
  • entry of bacterium into host cell Source: AgBase
  • growth Source: MTBBASE
  • lipid A biosynthetic process Source: UniProtKB-UniPathway
  • lipopolysaccharide biosynthetic process Source: InterPro
  • peptidoglycan biosynthetic process Source: UniProtKB-HAMAP
  • regulation of cell shape Source: UniProtKB-KW
  • UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-5176-MONOMER.
UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein GlmUUniRule annotation
Including the following 2 domains:
UDP-N-acetylglucosamine pyrophosphorylaseUniRule annotation (EC:2.7.7.23UniRule annotation2 Publications)
Alternative name(s):
N-acetylglucosamine-1-phosphate uridyltransferaseUniRule annotation
Glucosamine-1-phosphate N-acetyltransferaseUniRule annotation (EC:2.3.1.157UniRule annotation2 Publications)
Gene namesi
Name:glmUUniRule annotation
Ordered Locus Names:Rv1018c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1018c.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1293297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002338022 – 495Bifunctional protein GlmUAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Cross-linki362Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Post-translational modificationi

Phosphorylated at the C-terminal domain by PknB. The phosphorylation is required for acetyltransferase activity, but does not affect uridyltransferase activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP9WMN3.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CXCL8P101453EBI-11740532,EBI-3917999From a different organism.

Protein-protein interaction databases

IntActiP9WMN3. 1 interactor.
STRINGi83332.Rv1018c.

Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 13Combined sources7
Helixi18 – 20Combined sources3
Beta strandi22 – 24Combined sources3
Helixi26 – 28Combined sources3
Helixi36 – 47Combined sources12
Beta strandi50 – 56Combined sources7
Turni61 – 63Combined sources3
Helixi64 – 74Combined sources11
Beta strandi79 – 82Combined sources4
Helixi89 – 97Combined sources9
Beta strandi106 – 112Combined sources7
Helixi120 – 132Combined sources13
Beta strandi136 – 143Combined sources8
Beta strandi152 – 155Combined sources4
Beta strandi157 – 159Combined sources3
Beta strandi161 – 165Combined sources5
Helixi167 – 169Combined sources3
Helixi174 – 176Combined sources3
Beta strandi179 – 187Combined sources9
Helixi189 – 196Combined sources8
Beta strandi203 – 207Combined sources5
Helixi210 – 212Combined sources3
Helixi213 – 219Combined sources7
Beta strandi224 – 228Combined sources5
Helixi232 – 235Combined sources4
Helixi241 – 261Combined sources21
Beta strandi265 – 267Combined sources3
Helixi269 – 271Combined sources3
Beta strandi272 – 274Combined sources3
Beta strandi282 – 286Combined sources5
Beta strandi288 – 293Combined sources6
Beta strandi309 – 315Combined sources7
Beta strandi323 – 331Combined sources9
Beta strandi339 – 343Combined sources5
Beta strandi347 – 349Combined sources3
Beta strandi354 – 363Combined sources10
Beta strandi371 – 383Combined sources13
Beta strandi394 – 396Combined sources3
Beta strandi400 – 403Combined sources4
Beta strandi406 – 408Combined sources3
Beta strandi419 – 423Combined sources5
Helixi460 – 464Combined sources5
Helixi469 – 479Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QKXX-ray2.75A1-389[»]
3D8VX-ray2.55A1-495[»]
3D98X-ray2.50A1-495[»]
3DJ4X-ray2.38A1-495[»]
3FOQX-ray3.41A1-495[»]
3SPTX-ray2.33A1-495[»]
3ST8X-ray1.98A1-495[»]
4G3QX-ray1.90A1-495[»]
4G3SX-ray2.04A1-495[»]
4G87X-ray2.03A1-495[»]
4HCQX-ray2.60A1-495[»]
ProteinModelPortaliP9WMN3.
SMRiP9WMN3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 241PyrophosphorylaseUniRule annotationAdd BLAST240
Regioni12 – 15UDP-GlcNAc bindingUniRule annotation4 Publications4
Regioni88 – 89UDP-GlcNAc bindingUniRule annotation4 Publications2
Regioni112 – 114UDP-GlcNAc bindingUniRule annotation3 Publications3
Regioni242 – 262LinkerUniRule annotationAdd BLAST21
Regioni263 – 495N-acetyltransferaseUniRule annotationAdd BLAST233
Regioni397 – 398Acetyl-CoA bindingUniRule annotation2

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family.UniRule annotation
In the C-terminal section; belongs to the transferase hexapeptide repeat family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
KOiK04042.
OMAiFAHARPK.
PhylomeDBiP9WMN3.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P9WMN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFPGDTAVL VLAAGPGTRM RSDTPKVLHT LAGRSMLSHV LHAIAKLAPQ
60 70 80 90 100
RLIVVLGHDH QRIAPLVGEL ADTLGRTIDV ALQDRPLGTG HAVLCGLSAL
110 120 130 140 150
PDDYAGNVVV TSGDTPLLDA DTLADLIATH RAVSAAVTVL TTTLDDPFGY
160 170 180 190 200
GRILRTQDHE VMAIVEQTDA TPSQREIREV NAGVYAFDIA ALRSALSRLS
210 220 230 240 250
SNNAQQELYL TDVIAILRSD GQTVHASHVD DSALVAGVNN RVQLAELASE
260 270 280 290 300
LNRRVVAAHQ LAGVTVVDPA TTWIDVDVTI GRDTVIHPGT QLLGRTQIGG
310 320 330 340 350
RCVVGPDTTL TDVAVGDGAS VVRTHGSSSS IGDGAAVGPF TYLRPGTALG
360 370 380 390 400
ADGKLGAFVE VKNSTIGTGT KVPHLTYVGD ADIGEYSNIG ASSVFVNYDG
410 420 430 440 450
TSKRRTTVGS HVRTGSDTMF VAPVTIGDGA YTGAGTVVRE DVPPGALAVS
460 470 480 490
AGPQRNIENW VQRKRPGSPA AQASKRASEM ACQQPTQPPD ADQTP
Length:495
Mass (Da):51,584
Last modified:April 16, 2014 - v1
Checksum:iC14DC76BD6E5EC86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43768.1.
PIRiE70622.
RefSeqiNP_215534.1. NC_000962.3.
WP_003405267.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43768; CCP43768; Rv1018c.
GeneIDi886069.
KEGGimtu:Rv1018c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43768.1.
PIRiE70622.
RefSeqiNP_215534.1. NC_000962.3.
WP_003405267.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QKXX-ray2.75A1-389[»]
3D8VX-ray2.55A1-495[»]
3D98X-ray2.50A1-495[»]
3DJ4X-ray2.38A1-495[»]
3FOQX-ray3.41A1-495[»]
3SPTX-ray2.33A1-495[»]
3ST8X-ray1.98A1-495[»]
4G3QX-ray1.90A1-495[»]
4G3SX-ray2.04A1-495[»]
4G87X-ray2.03A1-495[»]
4HCQX-ray2.60A1-495[»]
ProteinModelPortaliP9WMN3.
SMRiP9WMN3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP9WMN3. 1 interactor.
STRINGi83332.Rv1018c.

Chemistry databases

ChEMBLiCHEMBL1293297.

Proteomic databases

PaxDbiP9WMN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43768; CCP43768; Rv1018c.
GeneIDi886069.
KEGGimtu:Rv1018c.

Organism-specific databases

TubercuListiRv1018c.

Phylogenomic databases

eggNOGiENOG4105CAJ. Bacteria.
COG1207. LUCA.
KOiK04042.
OMAiFAHARPK.
PhylomeDBiP9WMN3.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.
BioCyciMTBH37RV:G185E-5176-MONOMER.

Miscellaneous databases

PROiP9WMN3.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU. 1 hit.
InterProiIPR005882. Bifunctional_GlmU.
IPR001451. Hexapep.
IPR025877. MobA-like_NTP_Trfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF00132. Hexapep. 3 hits.
PF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF51161. SSF51161. 1 hit.
SSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR01173. glmU. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGLMU_MYCTU
AccessioniPrimary (citable) accession number: P9WMN3
Secondary accession number(s): L0T872, P96382, Q7D8Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, 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.