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Entry version 47 (25 May 2022)
Sequence version 1 (16 Apr 2014)
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Protein

Pantothenate synthetase

Gene

panC

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 condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.

1 Publication

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism.
Was identified as a high-confidence drug target.

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Pantothenate exhibits uncompetitive inhibition toward both D-pantoate and ATP, and non-competitive inhibition toward beta-alanine. AMPCPP exhibits competitive inhibition toward ATP, uncompetitive inhibition toward beta-alanine, and non-competitive inhibition toward D-pantoate. The enzyme is most active in the presence of magnesium or manganese. Other divalent cations (cobalt, nickel, zinc) are less effective.1 Publication

<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=130 µM for D-pantoate2 Publications
  2. KM=800 µM for beta-alanine2 Publications
  3. KM=2600 µM for ATP2 Publications
  4. KM=25.4 mM for 2-mercaptoethylamine2 Publications
  5. KM=36 mM for carbamate2 Publications
  6. KM=72 mM for 5-aminovalerate2 Publications
  7. KM=79 mM for methylamine2 Publications
  8. KM=84 mM for glycine2 Publications
  9. KM=93 mM for ethylamine2 Publications
  10. KM=103 mM for taurine2 Publications
  11. KM=108 mM for glycolate2 Publications
  12. KM=335 mM for gamma-aminobutyrate2 Publications
  13. KM=580 mM for gamma-amino-beta-hydroxybutyrate2 Publications

<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: (R)-pantothenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine. This subpathway is part of the pathway (R)-pantothenate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-pantothenate from (R)-pantoate and beta-alanine, the pathway (R)-pantothenate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei47Proton donor1
<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 sitei72Beta-alanine1
Binding sitei72Pantoate1
<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 bindingi88Magnesium1
Metal bindingi89Magnesium; via amide nitrogen1
Metal bindingi92Magnesium1
Binding sitei164Pantoate1
Binding sitei187ATP; via amide nitrogen and carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi40 – 47ATP1 Publication8
Nucleotide bindingi158 – 161ATP1 Publication4
Nucleotide bindingi195 – 198ATP1 Publication4

<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

GO - Biological processi

<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 functionLigase
Biological processPantothenate biosynthesis, Virulence
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.2.1, 3445

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

More...
UniPathwayi
UPA00028;UER00005

<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:
Pantothenate synthetase (EC:6.3.2.1)
Short name:
PS
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
<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:panC
Ordered Locus Names:Rv3602c
ORF Names:MTCY07H7B.20
<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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium 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
Rv3602c

<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

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

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Subcutaneous immunization with the double panD and panC bacterial disruption mutant protects mice for over a year against subsequent virulent M.tuberculosis (strain Erdman) infections; mice show mild lung inflammation and fibrosis despite a chronic bacterila infection. This is a promising attenuated vaccine strain.1 Publication

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Simultaneous disruption of panD and panC gives a mutant unable to grow in the absence of panothenate. The double mutant has a highly attenuated disease response in BALB/c and SCID mice; immunocompromised BALB/c SCID mice survive on average 36 weeks as opposed to 5 weeks for mice infected with wild-type bacteria, while immunocompetent BALB/c mice survive indefinitely. In wild-type mice bacteria grow for 3 weeks then undergo a steady decline, bacteria persist over 8 months in SCID mice (PubMed:12219086). The double mutant is sensitive to PZA but not POA in liquid culture, beta-alanine but not pantothenate antagonize the effect of PZA at pH 5.8 (PubMed:25246400).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi44H → A: More than 1000-fold reduction in activity and 52-fold decrease in adenylate formation. 1 Publication1
Mutagenesisi47H → A: More than 1000-fold reduction in activity and 60-fold decrease in adenylate formation. 10-fold decrease in the affinity for ATP. 1 Publication1
Mutagenesisi69N → A: More than 1000-fold reduction in activity and 50-fold decrease in adenylate formation. 1 Publication1
Mutagenesisi72Q → A: More than 1000-fold reduction in activity and 45-fold decrease in adenylate formation. 1 Publication1
Mutagenesisi77E → G: No effect. 1 Publication1
Mutagenesisi160K → A: More than 1000-fold reduction in activity and 50-fold decrease in the affinity for ATP. 1 Publication1
Mutagenesisi160K → C: More than 1000-fold reduction in activity and 120-fold decrease in adenylate formation. The enzymatic activity and the affinity for beta-alanine can be increased 10- and 3-fold, respectively, by alkylation of cysteine of mutant C-160. 1 Publication1
Mutagenesisi164Q → A: 50-fold reduction in activity and slight reduction in the affinity for beta-alanine. 30- and 40-fold decrease in adenylate formation and pantothenate formation, respectively. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6069

Drug and drug target database

More...
DrugBanki
DB01930, 2,4-Dihydroxy-3,3-Dimethyl-Butyrate
DB02596, alpha,beta-Methyleneadenosine 5'-triphosphate
DB03107, beta-Alanine
DB02694, Pantoyl Adenylate

<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 sources1 Publication
<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_00001282452 – 309Pantothenate synthetaseAdd BLAST308

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

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P9WIL5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P9WIL5

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv3602c

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P9WIL5

<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

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P9WIL5

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

More...
SMRi
P9WIL5

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

<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

Belongs to the pantothenate synthetase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0414, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
CNHKLEP

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P9WIL5

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00560, PanC, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1300.10, 1 hit
3.40.50.620, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00158, PanC, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003721, Pantoate_ligase
IPR042176, Pantoate_ligase_C
IPR014729, Rossmann-like_a/b/a_fold

The PANTHER Classification System

More...
PANTHERi
PTHR21299:SF1, PTHR21299:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02569, Pantoate_ligase, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00018, panC, 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.

P9WIL5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTIPAFHPGE LNVYSAPGDV ADVSRALRLT GRRVMLVPTM GALHEGHLAL
60 70 80 90 100
VRAAKRVPGS VVVVSIFVNP MQFGAGEDLD AYPRTPDDDL AQLRAEGVEI
110 120 130 140 150
AFTPTTAAMY PDGLRTTVQP GPLAAELEGG PRPTHFAGVL TVVLKLLQIV
160 170 180 190 200
RPDRVFFGEK DYQQLVLIRQ LVADFNLDVA VVGVPTVREA DGLAMSSRNR
210 220 230 240 250
YLDPAQRAAA VALSAALTAA AHAATAGAQA ALDAARAVLD AAPGVAVDYL
260 270 280 290 300
ELRDIGLGPM PLNGSGRLLV AARLGTTRLL DNIAIEIGTF AGTDRPDGYR

AILESHWRN
Length:309
Mass (Da):32,678
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:iEB51DBE3485F970A
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 32545 Da. Determined by ESI. 1 Publication

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: CCP46425.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C70955

NCBI Reference Sequences

More...
RefSeqi
NP_218119.1, NC_000962.3
WP_003419526.1, NZ_NVQJ01000056.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
885459

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv3602c

<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: CCP46425.1
PIRiC70955
RefSeqiNP_218119.1, NC_000962.3
WP_003419526.1, NZ_NVQJ01000056.1

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
1MOPX-ray1.60A/B3-300[»]
1N2BX-ray1.70A/B3-300[»]
1N2EX-ray1.60A/B3-300[»]
1N2GX-ray1.80A/B3-300[»]
1N2HX-ray2.00A/B3-300[»]
1N2IX-ray1.70A/B3-300[»]
1N2JX-ray1.80A/B3-300[»]
1N2OX-ray2.10A/B3-300[»]
2A7XX-ray1.70A3-300[»]
2A84X-ray1.55A3-300[»]
2A86X-ray1.85A/B3-300[»]
2A88X-ray1.70A3-300[»]
3COVX-ray1.50A/B3-300[»]
3COWX-ray1.80A/B3-300[»]
3COYX-ray2.03A/B3-300[»]
3COZX-ray2.00A/B3-300[»]
3IMCX-ray1.60A/B3-300[»]
3IMEX-ray2.39A/B3-300[»]
3IMGX-ray1.80A/B3-300[»]
3IOBX-ray1.80A/B3-300[»]
3IOCX-ray2.50A/B3-300[»]
3IODX-ray1.75A/B3-300[»]
3IOEX-ray1.95A/B3-300[»]
3ISJX-ray2.20A/B3-300[»]
3IUBX-ray1.50A/B3-301[»]
3IUEX-ray1.73A/B3-301[»]
3IVCX-ray2.13A/B3-301[»]
3IVGX-ray1.95A/B3-301[»]
3IVXX-ray1.73A/B3-301[»]
3LE8X-ray1.70A/B3-300[»]
4DDHX-ray2.07A/B3-301[»]
4DDKX-ray1.75A/B3-301[»]
4DDMX-ray1.83A/B3-301[»]
4DE5X-ray2.25A/B3-301[»]
4EF6X-ray1.94A/B3-300[»]
4EFKX-ray1.70A/B3-300[»]
4FZJX-ray1.63A/B3-301[»]
4G5FX-ray2.33A/B3-309[»]
4G5YX-ray1.80A/B3-300[»]
AlphaFoldDBiP9WIL5
SMRiP9WIL5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3602c

Chemistry databases

BindingDBiP9WIL5
ChEMBLiCHEMBL6069
DrugBankiDB01930, 2,4-Dihydroxy-3,3-Dimethyl-Butyrate
DB02596, alpha,beta-Methyleneadenosine 5'-triphosphate
DB03107, beta-Alanine
DB02694, Pantoyl Adenylate

PTM databases

iPTMnetiP9WIL5

Proteomic databases

PaxDbiP9WIL5

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
885459

Genome annotation databases

GeneIDi885459
KEGGimtu:Rv3602c

Organism-specific databases

TubercuListiRv3602c

Phylogenomic databases

eggNOGiCOG0414, Bacteria
OMAiCNHKLEP
PhylomeDBiP9WIL5

Enzyme and pathway databases

UniPathwayiUPA00028;UER00005
BRENDAi6.3.2.1, 3445

Family and domain databases

CDDicd00560, PanC, 1 hit
Gene3Di3.30.1300.10, 1 hit
3.40.50.620, 1 hit
HAMAPiMF_00158, PanC, 1 hit
InterProiView protein in InterPro
IPR003721, Pantoate_ligase
IPR042176, Pantoate_ligase_C
IPR014729, Rossmann-like_a/b/a_fold
PANTHERiPTHR21299:SF1, PTHR21299:SF1, 1 hit
PfamiView protein in Pfam
PF02569, Pantoate_ligase, 1 hit
TIGRFAMsiTIGR00018, panC, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiPANC_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: P9WIL5
Secondary accession number(s): L0TG74, O06280, P0A5R0
<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: May 25, 2022
This is version 47 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, Direct protein sequencing, 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
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