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Entry version 58 (18 Sep 2019)
Sequence version 1 (03 Oct 2012)
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Protein

Dihydrofolate synthase/folylpolyglutamate synthase

Gene

folC

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 addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu) (PubMed:23118010). Also catalyzes successive additions of L-glutamate to tetrahydrofolate, leading to folylpolyglutamate derivatives (By similarity).By similarity1 Publication
Is involved in the bioactivation of the antituberculous drug para-aminosalicylic acid (PAS). Is able to use hydroxy-dihydropteroate (H2PtePAS) as substrate, which is the product formed by the action of DHPS (FolP1) on PAS, leading to hydroxy-dihydrofolate (H2PtePAS-Glu). This compound inhibits dihydrofolate reductase DHFR (DfrA), the next enzyme in the folate pathway, and thus disrupts the folate-dependent metabolic pathways.1 Publication1 Publication

Miscellaneous

Mutations within this gene in the H2Pte binding pocket are responsible for PAS resistance in M.tuberculosis clinical isolates and laboratory strains. FolC-linked PAS resistance is mediated by altered substrate specificity that results in the failure to generate levels of H2PtePAS-Glu that are necessary to inhibit DHFR (DfrA); therefore, a blockage of PAS bioactivation causes PAS resistance.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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+By similarityNote: Binds 2 Mg2+ ions per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolate biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Dihydropteroate synthase (folP1)
  2. Dihydrofolate synthase/folylpolyglutamate synthase (folC)
This subpathway is part of the pathway tetrahydrofolate 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 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Pathwayi: tetrahydrofolylpolyglutamate biosynthesis

This protein is involved in the pathway tetrahydrofolylpolyglutamate biosynthesis, which is part of Cofactor biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway tetrahydrofolylpolyglutamate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi76Magnesium 11 Publication1
Metal bindingi98Magnesium 11 Publication1
Metal bindingi174Magnesium 11 Publication1
Metal bindingi201Magnesium 21 Publication1
Metal bindingi203Magnesium 21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei301ATPCombined sources1 Publication1
Binding sitei338ATPCombined sources1 Publication1
Metal bindingi384Magnesium 21 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi74 – 77ATPCombined sources1 Publication4
Nucleotide bindingi351 – 354ATPCombined sources1 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 processAntibiotic resistance, Folate biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MTBH37RV:G185E-6679-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.2.12 3445

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

More...
UniPathwayi
UPA00077;UER00157
UPA00850

<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_and_taxonomy_section">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:
Dihydrofolate synthase/folylpolyglutamate synthase1 Publication (EC:6.3.2.122 Publications, EC:6.3.2.17By similarity)
Short name:
DHFS / FPGS
Alternative name(s):
Folylpoly-gamma-glutamate synthetase
Tetrahydrofolylpolyglutamate synthase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:folCImported
Ordered Locus Names:Rv2447cImported, LH57_13380Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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
Rv2447c

<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

<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 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

Cells lacking this gene display impaired growth.1 Publication

<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 ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004390401 – 487Dihydrofolate synthase/folylpolyglutamate synthaseAdd BLAST487

Proteomic databases

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

More...
PaxDbi
I6Y0R5

PRoteomics IDEntifications database

More...
PRIDEi
I6Y0R5

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv2447c

<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

3D structure databases

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

More...
SMRi
I6Y0R5

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>Regioni44 – 467,8-dihydropteroate bindingBy similarity3
Regioni150 – 1537,8-dihydropteroate bindingBy similarity4
Regioni181 – 1837,8-dihydropteroate bindingBy similarity3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Is folded into two distinct domains, an N-terminal ATPase domain and a C-terminal Rossmann-fold domain, which are joined by a flexible linker.1 Publication

<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 folylpolyglutamate synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DPM Bacteria
COG0285 LUCA

KEGG Orthology (KO)

More...
KOi
K11754

Identification of Orthologs from Complete Genome Data

More...
OMAi
YFEMGTL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
I6Y0R5

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1190.10, 1 hit
3.90.190.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001645 Folylpolyglutamate_synth
IPR018109 Folylpolyglutamate_synth_CS
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen

The PANTHER Classification System

More...
PANTHERi
PTHR11136 PTHR11136, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01499 folC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01012 FOLYLPOLYGLU_SYNT_2, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

I6Y0R5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNSTNSGPPD SGSATGVVPT PDEIASLLQV EHLLDQRWPE TRIDPSLTRI
60 70 80 90 100
SALMDLLGSP QRSYPSIHIA GTNGKTSVAR MVDALVTALH RRTGRTTSPH
110 120 130 140 150
LQSPVERISI DGKPISPAQY VATYREIEPL VALIDQQSQA SAGKGGPAMS
160 170 180 190 200
KFEVLTAMAF AAFADAPVDV AVVEVGMGGR WDATNVINAP VAVITPISID
210 220 230 240 250
HVDYLGADIA GIAGEKAGII TRAPDGSPDT VAVIGRQVPK VMEVLLAESV
260 270 280 290 300
RADASVARED SEFAVLRRQI AVGGQVLQLQ GLGGVYSDIY LPLHGEHQAH
310 320 330 340 350
NAVLALASVE AFFGAGAQRQ LDGDAVRAGF AAVTSPGRLE RMRSAPTVFI
360 370 380 390 400
DAAHNPAGAS ALAQTLAHEF DFRFLVGVLS VLGDKDVDGI LAALEPVFDS
410 420 430 440 450
VVVTHNGSPR ALDVEALALA AGERFGPDRV RTAENLRDAI DVATSLVDDA
460 470 480
AADPDVAGDA FSRTGIVITG SVVTAGAART LFGRDPQ
Length:487
Mass (Da):50,779
Last modified:October 3, 2012 - 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:i77D3A4E3D2DC59D0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti40E → A in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility, confirmimg that this mutation confers high level resistance to PAS. 1 Publication1
Natural varianti40E → G in clinical isolates: Q274 and 501063; PAS-resistant; complementation with wild-type folC restores PAS susceptibility. 1 Publication1
Natural varianti43I → A in clinical isolate: Q36; PAS-resistant; complementation with wild-type folC restores PAS susceptibility. 1 Publication1
Natural varianti43I → T in clinical isolates: Q449 and 1314; PAS-resistant; complementation with wild-type folC restores PAS susceptibility; 7-fold reduction in DHFS activity relative to wild-type; loss of the ability to glutaminate H2PtePAS. 1 Publication1
Natural varianti73N → S in a spontaneous PAS-resistant mutant strain. 1 Publication1
Natural varianti150S → G in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility. 1 Publication1
Natural varianti152F → S in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility. 1 Publication1
Natural varianti153E → A in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility; 5-fold reduction in DHFS activity relative to wild-type; loss of the ability to glutaminate H2PtePAS. 1 Publication1
Natural varianti153E → G in a spontaneous PAS-resistant mutant strain; complementation with wild-type folC restores PAS susceptibility. 1 Publication1

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: CCP45240.1
CP009480 Genomic DNA Translation: AIR15214.1

NCBI Reference Sequences

More...
RefSeqi
NP_216963.1, NC_000962.3
WP_003899324.1, NZ_NVQJ01000024.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AIR15214; AIR15214; LH57_13380
CCP45240; CCP45240; Rv2447c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
885902

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2447c
mtv:RVBD_2447c

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|83332.111.peg.2739

<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: CCP45240.1
CP009480 Genomic DNA Translation: AIR15214.1
RefSeqiNP_216963.1, NC_000962.3
WP_003899324.1, NZ_NVQJ01000024.1

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
2VORX-ray2.30A1-487[»]
2VOSX-ray2.00A1-487[»]
SMRiI6Y0R5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2447c

Proteomic databases

PaxDbiI6Y0R5
PRIDEiI6Y0R5

Genome annotation databases

EnsemblBacteriaiAIR15214; AIR15214; LH57_13380
CCP45240; CCP45240; Rv2447c
GeneIDi885902
KEGGimtu:Rv2447c
mtv:RVBD_2447c
PATRICifig|83332.111.peg.2739

Organism-specific databases

TubercuListiRv2447c

Phylogenomic databases

eggNOGiENOG4105DPM Bacteria
COG0285 LUCA
KOiK11754
OMAiYFEMGTL
PhylomeDBiI6Y0R5

Enzyme and pathway databases

UniPathwayiUPA00077;UER00157
UPA00850
BioCyciMTBH37RV:G185E-6679-MONOMER
BRENDAi6.3.2.12 3445

Family and domain databases

Gene3Di3.40.1190.10, 1 hit
3.90.190.20, 1 hit
InterProiView protein in InterPro
IPR001645 Folylpolyglutamate_synth
IPR018109 Folylpolyglutamate_synth_CS
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen
PANTHERiPTHR11136 PTHR11136, 1 hit
PfamiView protein in Pfam
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit
SUPFAMiSSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit
TIGRFAMsiTIGR01499 folC, 1 hit
PROSITEiView protein in PROSITE
PS01012 FOLYLPOLYGLU_SYNT_2, 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 nameiFOLC_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: I6Y0R5
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2017
Last sequence update: October 3, 2012
Last modified: September 18, 2019
This is version 58 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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