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Entry version 75 (02 Jun 2021)
Sequence version 1 (03 Oct 2012)
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Protein

Polyketide synthase Pks13

Gene

pks13

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

Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:23770708, PubMed:25467124).

Forms, with FadD32, the initiation module of the mycolic condensation system (PubMed:19436070, PubMed:19477415, PubMed:25467124).

Synthesizes, in coupled reaction with FadD32, the biosynthetic precursors of mycolic acids, alpha-alkyl beta-ketoacids, via the condensation of two long chain fatty acid derivatives, a very long meromycoloyl-AMP and a shorter 2-carboxyacyl-CoA (PubMed:19436070, PubMed:25467124).

The acyl chain of the acyl-AMP produced by FadD32 is specifically transferred onto the N-terminal ACP domain of Pks13, and then transferred onto the KS domain. The extender unit carboxyacyl-CoA is specifically loaded onto the AT domain, which catalyzes the covalent attachment of the carboxyacyl chain to its active site, and its subsequent transfer onto the P-pant arm of the C-terminal ACP domain. The KS domain catalyzes the condensation between the two loaded fatty acyl chains to produce an alpha-alkyl beta-ketothioester linked to the C-ACP domain (PubMed:19436070).

Then, the thioesterase-like domain acts as a transacylase and is responsible for both the release and the transfer of the alpha-alkyl beta-ketoacyl chain onto a polyol acceptor molecule, particularly trehalose, leading to the formation of the trehalose monomycolate precursor (PubMed:25467124).

4 Publications

Miscellaneous

Identified as a drug target (PubMed:23770708, PubMed:28669536, PubMed:29328655, PubMed:30875203). Fatty acyl-AMP loading is inhibited by thiophene (TP) compounds, which kill Mycobacterium tuberculosis. Overexpression of wild-type Pks13 results in TP resistance, and overexpression of the F79S mutant confers high resistance (PubMed:23770708). Structure-guided methods identified a highly potent and very safe lead compound, TAM16, a benzofuran class inhibitor that targets the thioesterase activity (PubMed:28669536). The thioesterase-like domain is inhibited by coumestan derivatives that possess excellent anti-tuberculosis activity against both the drug-susceptible and drug-resistant Mtb strains (PubMed:29328655, PubMed:30875203).4 Publications

<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

The presence of FadD32 is necessary for the transfer of the acyl chain from the AMP carrier onto Pks13.1 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: mycolic acid biosynthesis

This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.3 Publications
View all proteins of this organism that are known to be involved in the pathway mycolic acid biosynthesis and in Lipid metabolism.

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 sitei287Acyl-thioester intermediate; for beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei801Acyl-ester intermediate; for acyltransferase activity1 Publication1
Active sitei1533For thioesterase-like activity1 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

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 functionAcyltransferase, Multifunctional enzyme, Transferase
Biological processFatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00915

<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:
Polyketide synthase Pks13Curated (EC:2.3.1.-2 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:pks13Imported
Ordered Locus Names:Rv3800cImported
<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
Rv3800c

<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

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>Mutagenesisi79F → S: Confers thiophene resistance. 1 Publication1
Mutagenesisi1533S → A: Cannot form alpha-alkyl beta-ketoacids derivatives. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4105939

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004515881 – 1733Polyketide synthase Pks13Add BLAST1733

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 residuei55O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1
Modified residuei1266O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1

<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

4'-phosphopantetheine is transferred from CoA to specific serines of apo-Pks13 by PptT.2 Publications

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
I6X8D2

PRoteomics IDEntifications database

More...
PRIDEi
I6X8D2

<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

Protein interaction database and analysis system

More...
IntActi
I6X8D2, 1 interactor

STRING: functional protein association networks

More...
STRINGi
83332.Rv3800c

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
I6X8D2

<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

11733
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
I6X8D2

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini17 – 95Carrier 1PROSITE-ProRule annotationAdd BLAST79
Domaini1232 – 1309Carrier 2PROSITE-ProRule annotationAdd BLAST78

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>Regioni118 – 539Beta-ketoacyl synthaseCuratedAdd BLAST422
Regioni548 – 567DisorderedSequence analysisAdd BLAST20
Regioni713 – 1034AcyltransferaseCuratedAdd BLAST322
Regioni1344 – 1368DisorderedSequence analysisAdd BLAST25
Regioni1470 – 1563Thioesterase-likeCuratedAdd BLAST94

<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

Made of a minimal module holding ketosynthase (KS), acyltransferase (AT), and C-terminal acyl carrier protein (C-ACP) domains, and additional N-terminal ACP (N-ACP) and C-terminal thioesterase-like domains.1 Publication1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0236, Bacteria
COG3319, Bacteria
COG3321, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
QLYVHGH

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 2 hits
3.40.47.10, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058, AB_hydrolase
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR001031, Thioesterase
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF00550, PP-binding, 2 hits
PF00975, Thioesterase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 2 hits
SSF52151, SSF52151, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 2 hits

<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.

I6X8D2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADVAESQEN APAERAELTV PEMRQWLRNW VGKAVGKAPD SIDESVPMVE
60 70 80 90 100
LGLSSRDAVA MAADIEDLTG VTLSVAVAFA HPTIESLATR IIEGEPETDL
110 120 130 140 150
AGDDAEDWSR TGPAERVDIA IVGLSTRFPG EMNTPEQTWQ ALLEGRDGIT
160 170 180 190 200
DLPDGRWSEF LEEPRLAARV AGARTRGGYL KDIKGFDSEF FAVAKTEADN
210 220 230 240 250
IDPQQRMALE LTWEALEHAR IPASSLRGQA VGVYIGSSTN DYSFLAVSDP
260 270 280 290 300
TVAHPYAITG TSSSIIANRV SYFYDFHGPS VTIDTACSSS LVAIHQGVQA
310 320 330 340 350
LRNGEADVVV AGGVNALITP MVTLGFDEIG AVLAPDGRIK SFSADADGYT
360 370 380 390 400
RSEGGGMLVL KRVDDARRDG DAILAVIAGS AVNHDGRSNG LIAPNQDAQA
410 420 430 440 450
DVLRRAYKDA GIDPRTVDYI EAHGTGTILG DPIEAEALGR VVGRGRPADR
460 470 480 490 500
PALLGAVKTN VGHLESAAGA ASMAKVVLAL QHDKLPPSIN FAGPSPYIDF
510 520 530 540 550
DAMRLKMITT PTDWPRYGGY ALAGVSSFGF GGANAHVVVR EVLPRDVVEK
560 570 580 590 600
EPEPEPEPKA AAEPAEAPTL AGHALRFDEF GNIITDSAVA EEPEPELPGV
610 620 630 640 650
TEEALRLKEA ALEELAAQEV TAPLVPLAVS AFLTSRKKAA AAELADWMQS
660 670 680 690 700
PEGQASSLES IGRSLSRRNH GRSRAVVLAH DHDEAIKGLR AVAAGKQAPN
710 720 730 740 750
VFSVDGPVTT GPVWVLAGFG AQHRKMGKSL YLRNEVFAAW IEKVDALVQD
760 770 780 790 800
ELGYSVLELI LDDAQDYGIE TTQVTIFAIQ IALGELLRHH GAKPAAVIGQ
810 820 830 840 850
SLGEAASAYF AGGLSLRDAT RAICSRSHLM GEGEAMLFGE YIRLMALVEY
860 870 880 890 900
SADEIREVFS DFPDLEVCVY AAPTQTVIGG PPEQVDAILA RAEAEGKFAR
910 920 930 940 950
KFATKGASHT SQMDPLLGEL TAELQGIKPT SPTCGIFSTV HEGRYIKPGG
960 970 980 990 1000
EPIHDVEYWK KGLRHSVYFT HGIRNAVDSG HTTFLELAPN PVALMQVALT
1010 1020 1030 1040 1050
TADAGLHDAQ LIPTLARKQD EVSSMVSTMA QLYVYGHDLD IRTLFSRASG
1060 1070 1080 1090 1100
PQDYANIPPT RFKRKEHWLP AHFSGDGSTY MPGTHVALPD GRHVWEYAPR
1110 1120 1130 1140 1150
DGNVDLAALV RAAAAHVLPD AQLTAAEQRA VPGDGARLVT TMTRHPGGAS
1160 1170 1180 1190 1200
VQVHARIDES FTLVYDALVS RAGSESVLPT AVGAATAIAV ADGAPVAPET
1210 1220 1230 1240 1250
PAEDADAETL SDSLTTRYMP SGMTRWSPDS GETIAERLGL IVGSAMGYEP
1260 1270 1280 1290 1300
EDLPWEVPLI ELGLDSLMAV RIKNRVEYDF DLPPIQLTAV RDANLYNVEK
1310 1320 1330 1340 1350
LIEYAVEHRD EVQQLHEHQK TQTAEEIARA QAELLHGKVG KTEPVDSEAG
1360 1370 1380 1390 1400
VALPSPQNGE QPNPTGPALN VDVPPRDAAE RVTFATWAIV TGKSPGGIFN
1410 1420 1430 1440 1450
ELPRLDDEAA AKIAQRLSER AEGPITAEDV LTSSNIEALA DKVRTYLEAG
1460 1470 1480 1490 1500
QIDGFVRTLR ARPEAGGKVP VFVFHPAGGS TVVYEPLLGR LPADTPMYGF
1510 1520 1530 1540 1550
ERVEGSIEER AQQYVPKLIE MQGDGPYVLV GWSLGGVLAY ACAIGLRRLG
1560 1570 1580 1590 1600
KDVRFVGLID AVRAGEEIPQ TKEEIRKRWD RYAAFAEKTF NVTIPAIPYE
1610 1620 1630 1640 1650
QLEELDDEGQ VRFVLDAVSQ SGVQIPAGII EHQRTSYLDN RAIDTAQIQP
1660 1670 1680 1690 1700
YDGHVTLYMA DRYHDDAIMF EPRYAVRQPD GGWGEYVSDL EVVPIGGEHI
1710 1720 1730
QAIDEPIIAK VGEHMSRALG QIEADRTSEV GKQ
Length:1,733
Mass (Da):186,446
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:iD6D933468481E86A
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 varianti1640N → K Coumestan resistant. 1 Publication1
Natural varianti1640N → S Coumestan resistant. 1 Publication1
Natural varianti1644D → G Coumestan resistant. 1 Publication1
Natural varianti1667A → V Coumestan resistant. 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: CCP46629.1

NCBI Reference Sequences

More...
RefSeqi
NP_218317.1, NC_000962.3
WP_003902557.1, NZ_NVQJ01000022.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
886133

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv3800c

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|83332.111.peg.4225

<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: CCP46629.1
RefSeqiNP_218317.1, NC_000962.3
WP_003902557.1, NZ_NVQJ01000022.1

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
3TZWX-ray2.60A576-1062[»]
3TZXX-ray2.30A/B576-1062[»]
3TZYX-ray2.20A/B576-1062[»]
3TZZX-ray2.49A/B576-1062[»]
5V3WX-ray1.72A/B1451-1733[»]
5V3XX-ray1.94A/B1451-1733[»]
5V3YX-ray1.98A/B1451-1733[»]
5V3ZX-ray1.88A/B1451-1733[»]
5V40X-ray1.99A/B1451-1733[»]
5V41X-ray2.05A/B1451-1733[»]
5V42X-ray1.99A/B1451-1733[»]
5XUOX-ray2.59A717-827[»]
6C4QX-ray1.16A1-100[»]
6C4VX-ray1.90A1349-1461[»]
6D8IX-ray1.65A10-93[»]
6D8JX-ray1.63A10-93[»]
SMRiI6X8D2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiI6X8D2, 1 interactor
STRINGi83332.Rv3800c

Chemistry databases

BindingDBiI6X8D2
ChEMBLiCHEMBL4105939

Proteomic databases

PaxDbiI6X8D2
PRIDEiI6X8D2

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
886133

Genome annotation databases

GeneIDi886133
KEGGimtu:Rv3800c
PATRICifig|83332.111.peg.4225

Organism-specific databases

TubercuListiRv3800c

Phylogenomic databases

eggNOGiCOG0236, Bacteria
COG3319, Bacteria
COG3321, Bacteria
OMAiQLYVHGH

Enzyme and pathway databases

UniPathwayiUPA00915

Family and domain databases

Gene3Di1.10.1200.10, 2 hits
3.40.47.10, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR001031, Thioesterase
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF00550, PP-binding, 2 hits
PF00975, Thioesterase, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 2 hits
SUPFAMiSSF47336, SSF47336, 2 hits
SSF52151, SSF52151, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 2 hits

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 nameiPKS13_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: I6X8D2
<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: December 2, 2020
Last sequence update: October 3, 2012
Last modified: June 2, 2021
This is version 75 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
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