Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P9WMN3 (GLMU_MYCTU)

Entry version 48 (02 Dec 2020)
Sequence version 1 (16 Apr 2014)
Previous versions | rss
Add a publicationFeedback
Protein

Bifunctional protein GlmU

Gene

glmU

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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)
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)
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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei26UDP-GlcNAcUniRule annotation1 Publication1
Binding sitei83UDP-GlcNAcUniRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
Biological processCell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P9WMN3

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00113;UER00532
UPA00113;UER00533
UPA00973

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:glmUUniRule annotation
Ordered Locus Names:Rv1018c
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83332 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Mycobacterium tuberculosis strain H37Rv genome database

More...TubercuListi		Rv1018c

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1293297

DrugCentral

More...DrugCentrali		P9WMN3

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002338022 – 495Bifunctional protein GlmUAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylthreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki362Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P9WMN3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P9WMN3

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer.

UniRule annotation4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P9WMN3, 1 interactor

STRING: functional protein association networks

More...STRINGi		83332.Rv1018c

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P9WMN3

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1207, Bacteria

Identification of Orthologs from Complete Genome Data

More...OMAi		TAIVEHK

Database for complete collections of gene phylogenies

More...PhylomeDBi		P9WMN3

Family and domain databases

Conserved Domains Database

More...CDDi		cd03353, LbH_GlmU_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01631, GlmU, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005882, Bifunctional_GlmU
IPR038009, GlmU_C_LbH
IPR001451, Hexapep
IPR025877, MobA-like_NTP_Trfase
IPR029044, Nucleotide-diphossugar_trans
IPR011004, Trimer_LpxA-like_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00132, Hexapep, 3 hits
PF12804, NTP_transf_3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51161, SSF51161, 1 hit
SSF53448, SSF53448, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01173, glmU, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC14DC76BD6E5EC86
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP43768.1

Protein sequence database of the Protein Information Resource

More...PIRi		E70622

NCBI Reference Sequences

More...RefSeqi		NP_215534.1, NC_000962.3
WP_003405267.1, NZ_NVQJ01000018.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CCP43768; CCP43768; Rv1018c

Database of genes from NCBI RefSeq genomes

More...GeneIDi		23492850
886069

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mtu:Rv1018c
mtv:RVBD_1018c

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_NVQJ01000018.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
4G3PX-ray2.47A1-495[»]
4G3QX-ray1.90A1-495[»]
4G3SX-ray2.04A1-495[»]
4G87X-ray2.03A1-495[»]
4HCQX-ray2.60A1-495[»]
SMRiP9WMN3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP9WMN3, 1 interactor
STRINGi83332.Rv1018c

Chemistry databases

ChEMBLiCHEMBL1293297
DrugCentraliP9WMN3

PTM databases

iPTMnetiP9WMN3

Proteomic databases

PaxDbiP9WMN3

Genome annotation databases

EnsemblBacteriaiCCP43768; CCP43768; Rv1018c
GeneIDi23492850
886069
KEGGimtu:Rv1018c
mtv:RVBD_1018c

Organism-specific databases

TubercuListiRv1018c

Phylogenomic databases

eggNOGiCOG1207, Bacteria
OMAiTAIVEHK
PhylomeDBiP9WMN3

Enzyme and pathway databases

UniPathwayiUPA00113;UER00532
UPA00113;UER00533
UPA00973
SABIO-RKiP9WMN3

Miscellaneous databases

Protein Ontology

More...PROi		PR:P9WMN3

Family and domain databases

CDDicd03353, LbH_GlmU_C, 1 hit
Gene3Di3.90.550.10, 1 hit
HAMAPiMF_01631, GlmU, 1 hit
InterProiView protein in InterPro
IPR005882, Bifunctional_GlmU
IPR038009, GlmU_C_LbH
IPR001451, Hexapep
IPR025877, MobA-like_NTP_Trfase
IPR029044, Nucleotide-diphossugar_trans
IPR011004, Trimer_LpxA-like_sf
PfamiView protein in Pfam
PF00132, Hexapep, 3 hits
PF12804, NTP_transf_3, 1 hit
SUPFAMiSSF51161, SSF51161, 1 hit
SSF53448, SSF53448, 1 hit
TIGRFAMsiTIGR01173, glmU, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLMU_MYCTU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P9WMN3
Secondary accession number(s): L0T872, P96382, Q7D8Z8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: December 2, 2020
This is version 48 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again