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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261UDP-GlcNAcUniRule annotation1 Publication
Binding sitei83 – 831UDP-GlcNAcUniRule annotation2 Publications
Metal bindingi114 – 1141Magnesium or cobalt4 Publications
Binding sitei151 – 1511UDP-GlcNAc; via amide nitrogenUniRule annotation4 Publications
Binding sitei166 – 1661UDP-GlcNAcUniRule annotation4 Publications
Binding sitei181 – 1811UDP-GlcNAcUniRule annotation4 Publications
Metal bindingi239 – 2391Magnesium or cobalt4 Publications
Binding sitei239 – 2391UDP-GlcNAcUniRule annotation4 Publications
Binding sitei344 – 3441UDP-GlcNAcUniRule annotation2 Publications
Binding sitei362 – 3621UDP-GlcNAcUniRule annotation2 Publications
Active sitei374 – 3741Proton acceptorUniRule annotation1 Publication
Binding sitei377 – 3771UDP-GlcNAcUniRule annotation2 Publications
Binding sitei388 – 3881UDP-GlcNAcUniRule annotation1 Publication
Binding sitei391 – 3911Acetyl-CoA; via amide nitrogenUniRule annotation1 Publication
Binding sitei416 – 4161Acetyl-CoA; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei434 – 4341Acetyl-CoA; via amide nitrogen1 Publication

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

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

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

ChEMBLiCHEMBL1293297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 495494Bifunctional protein GlmUPRO_0000233802Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineCombined sources
Cross-linki362 – 362Isoglutamyl 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

Protein-protein interaction databases

STRINGi83332.Rv1018c.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi18 – 203Combined sources
Beta strandi22 – 243Combined sources
Helixi26 – 283Combined sources
Helixi36 – 4712Combined sources
Beta strandi50 – 567Combined sources
Turni61 – 633Combined sources
Helixi64 – 7411Combined sources
Beta strandi79 – 824Combined sources
Helixi89 – 979Combined sources
Beta strandi106 – 1127Combined sources
Helixi120 – 13213Combined sources
Beta strandi136 – 1438Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi161 – 1655Combined sources
Helixi167 – 1693Combined sources
Helixi174 – 1763Combined sources
Beta strandi179 – 1879Combined sources
Helixi189 – 1968Combined sources
Beta strandi203 – 2075Combined sources
Helixi210 – 2123Combined sources
Helixi213 – 2197Combined sources
Beta strandi224 – 2285Combined sources
Helixi232 – 2354Combined sources
Helixi241 – 26121Combined sources
Beta strandi265 – 2673Combined sources
Helixi269 – 2713Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi282 – 2865Combined sources
Beta strandi288 – 2936Combined sources
Beta strandi309 – 3157Combined sources
Beta strandi323 – 3319Combined sources
Beta strandi339 – 3435Combined sources
Beta strandi347 – 3493Combined sources
Beta strandi354 – 36310Combined sources
Beta strandi371 – 38313Combined sources
Beta strandi394 – 3963Combined sources
Beta strandi400 – 4034Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi419 – 4235Combined sources
Helixi460 – 4645Combined sources
Helixi469 – 47911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 241240PyrophosphorylaseUniRule annotationAdd
BLAST
Regioni12 – 154UDP-GlcNAc bindingUniRule annotation4 Publications
Regioni88 – 892UDP-GlcNAc bindingUniRule annotation4 Publications
Regioni112 – 1143UDP-GlcNAc bindingUniRule annotation3 Publications
Regioni242 – 26221LinkerUniRule annotationAdd
BLAST
Regioni263 – 495233N-acetyltransferaseUniRule annotationAdd
BLAST
Regioni397 – 3982Acetyl-CoA bindingUniRule annotation

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.
OMAiSITANYD.
PhylomeDBiP9WMN3.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
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
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. Positions 6-480.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1018c.

Chemistry

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.
OMAiSITANYD.
PhylomeDBiP9WMN3.

Enzyme and pathway databases

UniPathwayiUPA00113; UER00532.
UPA00113; UER00533.
UPA00973.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01631. GlmU.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. "Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis."
    Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H.
    PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUPYLATION AT LYS-362, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: ATCC 25618 / H37Rv.
  3. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.
  4. "Structure and function of GlmU from Mycobacterium tuberculosis."
    Zhang Z., Bulloch E.M., Bunker R.D., Baker E.N., Squire C.J.
    Acta Crystallogr. D 65:275-283(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
  5. "Structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group."
    Verma S.K., Jaiswal M., Kumar N., Parikh A., Nandicoori V.K., Prakash B.
    Acta Crystallogr. F 65:435-439(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.41 ANGSTROMS), SUBUNIT.
  6. "PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity."
    Parikh A., Verma S.K., Khan S., Prakash B., Nandicoori V.K.
    J. Mol. Biol. 386:451-464(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
  7. "Structure of Mycobacterium tuberculosis GlmU in complex with Acetyl CoA."
    Jagtap P.A., Prakash B.
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; ACETYL-COA AND MAGNESIUM IONS, COFACTOR, SUBUNIT.
  8. "Structural snapshots of Glmu from Mycobacterium tuberculosis."
    Jagtap P.A., Verma S.K., Prakash B.
    Submitted (JUL-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; MAGNESIUM AND COBALT IONS, COFACTOR.
  9. "Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases."
    Jagtap P.K., Verma S.K., Vithani N., Bais V.S., Prakash B.
    J. Mol. Biol. 425:1745-1759(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC; MAGNESIUM AND COBALT IONS, COFACTOR, REACTION MECHANISM.

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: February 17, 2016
This is version 21 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.