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Entry version 60 (07 Apr 2021)
Sequence version 1 (03 Oct 2012)
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Protein

Mycoketide-CoA synthase

Gene

pks12

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 synthesis of beta-D-mannosyl phosphomycoketide (MPM), an antigenic mycobacterial polyketide (PubMed:15611286, PubMed:18613748).

Binds a fatty acyl-CoA as a starter unit, and extends it by five rounds of alternative additions of malonyl-CoA and methylmalonyl-CoA extender units. Depending on the starter unit, the enzyme forms mycoketide-CoAs of different lengths (PubMed:15611286, PubMed:18613748).

Shows preference for small-/medium-chain starter fatty acyl substrates (PubMed:18613748).

Uses a hybrid modularly iterative mechanism, by forming a supramolecular assembly to perform repetitive cycles of iterations (PubMed:18613748).

2 Publications

Miscellaneous

The alkane moiety distinguishes these mycobacterial lipid antigens from mammalian mannosyl beta-1-phosphodolichol (MPD) and is necessary for activation of CD1c-restricted T cells.1 Publication

<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 the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism 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 sitei203Acyl-thioester intermediate; for beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation1
Active sitei650Acyl-ester intermediate; for acyltransferase 1 activityBy similarity1
Active sitei1828For beta-ketoacyl reductase 1 activityBy similarity1
Active sitei2226Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1
Active sitei2672Acyl-ester intermediate; for acyltransferase 2 activityBy similarity1
Active sitei3858For beta-ketoacyl reductase 2 activityBy similarity1

<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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G185E-6251-MONOMER

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

More...
UniPathwayi
UPA00199

<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:
Mycoketide-CoA synthaseCurated (EC:2.3.1.2952 Publications)
Alternative name(s):
Polyketide synthase Pks12Curated
<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:pks12Imported
Synonyms:msl61 Publication
Ordered Locus Names:Rv2048cImported
<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
Rv2048c

<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

Deletion of the gene completely abolishes the ability of the strain to activate CD1c-restricted T cells (PubMed:15611286). Growth of the mutant is attenuated in mouse alveolar macrophage cell line, and the virulence of the mutant in vivo is highly attenuated in a murine model (PubMed:12819062). Sirakova et al. showed that disruption of the gene causes a drastic decrease in the synthesis of dimycocerosyl phthiocerol (DIM), but Matsunaga et al. demonstrated later that DIM is produced by the disruption mutant (PubMed:12819062, PubMed:15611286).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>Mutagenesisi2226C → A: Loss of activity. 1 Publication1
Mutagenesisi2672S → A: Loss of activity. 1 Publication1

<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_00004515831 – 4151Mycoketide-CoA synthaseAdd BLAST4151

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 residuei1998O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei4030O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
I6XD69

PRoteomics IDEntifications database

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PRIDEi
I6XD69

<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

Forms a large supramolecular assembly mediated through specific interactions between the N- and C-terminus linkers.

1 Publication

<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

I6XD69
With#Exp.IntAct
itself2EBI-16359004,EBI-16359004

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
83332.Rv2048c

<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
I6XD69

Database of comparative protein structure models

More...
ModBasei
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>Domaini1963 – 2038Carrier 1PROSITE-ProRule annotationAdd BLAST76
Domaini3995 – 4070Carrier 2PROSITE-ProRule annotationAdd BLAST76

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>Regioni35 – 2038Module 1CuratedAdd BLAST2004
Regioni35 – 407Beta-ketoacyl synthase 1CuratedAdd BLAST373
Regioni559 – 880Acyltransferase 1CuratedAdd BLAST322
Regioni926 – 1194Dehydratase 1CuratedAdd BLAST269
Regioni1366 – 1671Enoyl reductase 1CuratedAdd BLAST306
Regioni1680 – 1858Beta-ketoacyl reductase 1CuratedAdd BLAST179
Regioni2057 – 4070Module 2CuratedAdd BLAST2014
Regioni2057 – 2430Beta-ketoacyl synthase 2CuratedAdd BLAST374
Regioni2582 – 2893Acyltransferase 2CuratedAdd BLAST312
Regioni2940 – 3215Dehydratase 2CuratedAdd BLAST276
Regioni3395 – 3701Enoyl reductase 2CuratedAdd BLAST307
Regioni3710 – 3888Beta-ketoacyl reductase 2CuratedAdd BLAST179

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili2 – 32Sequence analysisAdd BLAST31

<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

Contains 12 catalytic domains constituting two modules. Both modules contain a complete set of catalytic and auxiliary domains.1 Publication

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0604, Bacteria
COG3321, Bacteria

Identification of Orthologs from Complete Genome Data

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OMAi
PWRLGMS

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 2 hits
3.10.129.110, 2 hits
3.40.366.10, 2 hits
3.40.47.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013154, ADH_N
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698, Acyl_transf_1, 2 hits
PF08240, ADH_N, 1 hit
PF16197, KAsynt_C_assoc, 2 hits
PF00109, ketoacyl-synt, 2 hits
PF02801, Ketoacyl-synt_C, 2 hits
PF08659, KR, 2 hits
PF00550, PP-binding, 2 hits
PF14765, PS-DH, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827, PKS_AT, 2 hits
SM00826, PKS_DH, 2 hits
SM00829, PKS_ER, 2 hits
SM00825, PKS_KS, 2 hits
SM00823, PKS_PP, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 2 hits
SSF50129, SSF50129, 2 hits
SSF51735, SSF51735, 6 hits
SSF52151, SSF52151, 2 hits
SSF53901, SSF53901, 2 hits
SSF55048, SSF55048, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 2 hits
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 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.

I6XD69-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVDQLQHATE ALRKALVQVE RLKRTNRALL ERSSEPIAIV GMSCRFPGGV
60 70 80 90 100
DSPEGLWQMV ADARDVMSEF PTDRGWDLAG LFDPDPDVRH KSYARTGGFV
110 120 130 140 150
DGVADFDPAF FGISPSEALA MDPQHRMLLE LSWEALERAG IDPTGLRGSA
160 170 180 190 200
TGVFAGLIVG GYGMLAEEIE GYRLTGMTSS VASGRVAYVL GLEGPAVSVD
210 220 230 240 250
TACSSSLVAL HMAVGSLRSG ECDLALAGGV TVNATPTVFV EFSRHRGLAP
260 270 280 290 300
DGRCKPYAGR ADGVGWSEGG GMLVLQRLSD ARRLGHPVLA VVVGSAVNQD
310 320 330 340 350
GASNGLTAPN GPSQQRVVRA ALANAGLSAA EVDVVEGHGT GTTLGDPIEA
360 370 380 390 400
QALLATYGQD RGEPGEPLWL GSVKSNMGHT QAAAGVAGVI KMVLAMRHEL
410 420 430 440 450
LPATLHVDVP SPHVDWSAGA VELLTAPRVW PAGARTRRAG VSSFGISGTN
460 470 480 490 500
AHVIIEAVPV VPRREAGWAG PVVPWVVSAK SESALRGQAA RLAAYVRGDD
510 520 530 540 550
GLDVADVGWS LAGRSVFEHR AVVVGGDRDR LLAGLDELAG DQLGGSVVRG
560 570 580 590 600
TATAAGKTVF VFPGQGSQWL GMGIELLDTA PAFAQQIDAC AEAFAEFVDW
610 620 630 640 650
SLVDVLRGAP GAPGLDRVDV VQPVLFAVMV SLAELWKSVA VHPDAVIGHS
660 670 680 690 700
QGEIAAAYVA GALSLRDAAR VVTLRSKLLA GLAGPGGMVS IACGADQARD
710 720 730 740 750
LLAPFGDRVS IAVVNGPSAV VVSGEVGALE ELIAVCSTKE LRTRRIEVDY
760 770 780 790 800
ASHSVEVEAI RGPLAEALSG IEPRSTRTVF FSTVTGNRLD TAGLDADYWY
810 820 830 840 850
RNVRQTVLFD QAVRNACEQG YRTFIESSPH PALITGVEET FAACTDGDSE
860 870 880 890 900
AIVVPTLGRG DGGLHRFLLS AASAFVAGVA VNWRGTLDGA GYVELPTYAF
910 920 930 940 950
DKRRFWLSAE GSGADVSGLG LGASEHPLLG AVVDLPASGG VVLTGRLSPN
960 970 980 990 1000
VQPWLADHAV SDVVLFPGTG FVELAIRAGD EVGCSVLDEL TLAAPLLLPA
1010 1020 1030 1040 1050
TGSVAVQVVV DAGRDSNSRG VSIFSRADAQ AGWLLHAEGI LRPGSVEPGA
1060 1070 1080 1090 1100
DLSVWPPAGA VTVDVADGYE RLATRGYRYG PAFRGLTAMW ARGEEIFAEV
1110 1120 1130 1140 1150
RLPEAAGGVG GFGVHPALLD AVLHAVVIAG DPDELALPFA WQGVSLHATG
1160 1170 1180 1190 1200
ASAVRARIAP AGPSAVSVEL ADGLGLPVLS VASMVARPVT ERQLLAAVSG
1210 1220 1230 1240 1250
SGPDRLFEVI WSPASAATSP GPTPAYQIFE SVAADQDPVA GSYVRSHQAL
1260 1270 1280 1290 1300
AAVQSWLTDH ESGVLVVATR GAMALPREDV ADLAGAAVWG LVRSAQTEHP
1310 1320 1330 1340 1350
GRIVLVDSDA ATDDAAIAMA LATGEPQVVL RGGQVYTARV RGSRAADAIL
1360 1370 1380 1390 1400
VPPGDGPWRL GLGSAGTFEN LRLEPVPNAD APLGPGQVRV AMRAIAANFR
1410 1420 1430 1440 1450
DIMITLGMFT HDALLGGEGA GVVVEVGPGV TEFSVGDSVF GFFPDGSGTL
1460 1470 1480 1490 1500
VAGDVRLLLP MPADWSYAEA AAISAVFTTA YYAFIHLADV QPGQRVLIHA
1510 1520 1530 1540 1550
GTGGVGMAAV QLARHLGLEV FATASKGKWD TLRAMGFDDD HISDSRSLEF
1560 1570 1580 1590 1600
EDKFRAATGG RGFDVVLDSL AGEFVDASLR LVAPGGVFLE MGKTDIRDPG
1610 1620 1630 1640 1650
VIAQQYPGVR YRAFDLFEPG RPRMHQYMLE LATLFGDGVL RPLPVTTFDV
1660 1670 1680 1690 1700
RRAPAALRYL SQARHTGKVV MLMPGSWAAG TVLITGGTGM AGSAVARHVV
1710 1720 1730 1740 1750
ARHGVRNLVL VSRRGPDAPG AAELVAELAA AGAQVQVVAC DAADRAALAK
1760 1770 1780 1790 1800
VIADIPVQHP LSGVIHTAGA LDDAVVMSLT PDRVDVVLRS KVDAAWHLHE
1810 1820 1830 1840 1850
LTRDLDVSAF VMFSSMAGLV GSSGQANYAA ANSFLDALAA HRRAHGLPAI
1860 1870 1880 1890 1900
SLGWGLWDQA SAMTGGLDAA DLARLGREGV LALSTAEALE LFDTAMIVDE
1910 1920 1930 1940 1950
PFLAPARIDL TALRAHAVAV PPMFSDLASA PTRRQVDDSV AAAKSKSALA
1960 1970 1980 1990 2000
HRLHGLPEAE QHAVLLGLVR LHIATVLGNI TPEAIDPDKA FQDLGFDSLT
2010 2020 2030 2040 2050
AVEMRNRLKS ATGLSLSPTL IFDYPTPNRL ASYIRTELAG LPQEIKHTPA
2060 2070 2080 2090 2100
VRTTSEDPIA IVGMACRYPG GVNSPDDMWD MLIQGRDVLS EFPADRGWDL
2110 2120 2130 2140 2150
AGLYNPDPDA AGACYTRTGG FVDGVGDFDP AFFGVGPSEA LAMDPQHRML
2160 2170 2180 2190 2200
LELSWEALER AGIDPTGLRG SATGVFAGVM TQGYGMFAAE PVEGFRLTGQ
2210 2220 2230 2240 2250
LSSVASGRVA YVLGLEGPAV SVDTACSSSL VALHMAVGSL RSGECDLALA
2260 2270 2280 2290 2300
GGVTVNATPD IFVEFSRWRG LSPDGRCKAF AAAADGTGFS EGGGMLVLQR
2310 2320 2330 2340 2350
LSDARRLGHP VLAVVVGSAV NQDGASNGLT APNGPSQQRV VRAALANAGL
2360 2370 2380 2390 2400
SAAEVDVVEG HGTGTTLGDP IEAQALLATY GQDRGEPGEP LWLGSVKSNM
2410 2420 2430 2440 2450
GHTQAAAGVA GVIKMVLAMR HELLPATLHV DVPSPHVDWS AGAVELLTAP
2460 2470 2480 2490 2500
RVWPAGARTR RAGVSSFGIS GTNAHVIIEA VPVVPRREAG WAGPVVPWVV
2510 2520 2530 2540 2550
SAKSESALRG QAARLAAYVR GDDGLDVADV GWSLAGRSVF EHRAVVVGGD
2560 2570 2580 2590 2600
RDRLLAGLDE LAGDQLGGSV VRGTATAAGK TVFVFPGQGS QWLGMGMGLH
2610 2620 2630 2640 2650
AGYPVFAEAF NTVVGELDRH LLRPLREVMW GHDENLLNST EFAQPALFAV
2660 2670 2680 2690 2700
EVALFRLLGS WGVRPDFVMG HSIGELSAAH VAGVLSLENA AVLVAARGRL
2710 2720 2730 2740 2750
MQALPAGGAM VAVQAAEEEV RPLLSAEVDI AAVNGPASLV ISGAQNAVAA
2760 2770 2780 2790 2800
VADQLRADGR RVHQLAVSHA FHSPLMDPMI DEFAAVAAGI AIGRPTIGVI
2810 2820 2830 2840 2850
SNVTGQLAGD DFGSAAYWRR HIRQAVRFAD SVRFAQAAGG SRFLEVGPSG
2860 2870 2880 2890 2900
GLVASIEESL PDVAVTTMSA LRKDRPEPAT LTNAVAQGFV TGMDLDWRAV
2910 2920 2930 2940 2950
VGEAQFVELP TYAFQRRRFW LSGDGVAADA AGLGLAASEH ALLGAVIDLP
2960 2970 2980 2990 3000
ASGGVVLTGR LSPSVQGWLA DHSVAGVTIF PGAGFVELAI RAGDEVGCGV
3010 3020 3030 3040 3050
VDELTLAAPL VLPASGSVAV QVVVNGPDES GVRGVSVYSR GDVGTGWVLH
3060 3070 3080 3090 3100
AEGALRAGSA EPTADLAMWP PAGAVPVEVA DGYQQLAERG YGYGPAFRGL
3110 3120 3130 3140 3150
TAMWRRGDEV FAEVALPADA GVSVTGFGVH PVLLDAALHA VVLSAESAER
3160 3170 3180 3190 3200
GQGSVLVPFS WQGVSLHAAG ASAVRARIAP VGPSAVSIEL ADGLGLPVLS
3210 3220 3230 3240 3250
VASMLARPVT DQQLRAAVSS SGPDRLFEVT WSPQPSAAVE PLPVCAWGTT
3260 3270 3280 3290 3300
EDSAAVVFES VPLAGDVVAG VYAATSSVLD VLQSWLTRDG AGVLVVMTRG
3310 3320 3330 3340 3350
AVALPGEDVT DLAGAAVWGL VRSAQTEHPG RIVLVDSDAP LDDSALAAVV
3360 3370 3380 3390 3400
TTGEPQVLWR RGEVYTARVH GSRAVGGLLV PPSDRPWRLA MSTAGTFENL
3410 3420 3430 3440 3450
RLELIPDADA PLGPGQVRVA VSAIAANFRD VMIALGLYPD PDAVMGVEAC
3460 3470 3480 3490 3500
GVVIETSLNK GSFAVGDRVM GLFPEGTGTV ASTDQRLLVK VPAGWSHTAA
3510 3520 3530 3540 3550
ATTSVVFATA HYALVDLAAA RSGQRVLIHA GTGGVGMAAV QLARHLGLEV
3560 3570 3580 3590 3600
FATASKGKWD TLRAMGFDDD HISDSRSLEF EDKFRAATGG RGFDVVLDSL
3610 3620 3630 3640 3650
AGEFVDASLR LVAPGGVFLE MGKTDIRDPG VIAQQYPGVR YRAFDLFEPG
3660 3670 3680 3690 3700
PDRIAQILAE LATLFGDGVL RPLPVTTFDV RCAPAALRYL SQARHTGKVV
3710 3720 3730 3740 3750
MLMPGSWAAG TVLITGGTGM AGSAVARHVV ARHGVRNLVL VSRRGPDAPG
3760 3770 3780 3790 3800
AAELVAELAA AGAQVQVVAC DAADRAALAK VIADIPVQHP LSGVIHTAGA
3810 3820 3830 3840 3850
LDDAVVMSLT PDRVDVVLRS KVDAAWHLHE LTRDLDVSAF VMFSSMAGLV
3860 3870 3880 3890 3900
GSSGQANYAA ANSFLDALAA HRRAHGLPAI SLGWGLWDQA SAMTGGLATV
3910 3920 3930 3940 3950
DFKRFARDGI VAMSSADALQ LFDTAMIVDE PFMLPAHIDF AALKVKFDGG
3960 3970 3980 3990 4000
TLPPMFVDLI NAPTRRQVDD SLAAAKSKSA LLQRLEGLPE DEQHAVLLDL
4010 4020 4030 4040 4050
VRSHIATVLG SASPEAIDPD RAFQELGFDS LTAVEMRNRL KSATGLALSP
4060 4070 4080 4090 4100
TLIFDYPNSA ALAGYMRREL LGSSPQDTSA VAAGEAELQR IVASIPVKRL
4110 4120 4130 4140 4150
RQAGVLDLLL ALANETETSG QDPALAPTAE QEIADMDLDD LVNAAFRNDD

E
Length:4,151
Mass (Da):431,607
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:i433C816243C141B2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AL123456 Genomic DNA Translation: CCP44821.1

NCBI Reference Sequences

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RefSeqi
NP_216564.2, NC_000962.3
WP_010886138.1, NC_018143.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
888350

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mtu:Rv2048c

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|83332.111.peg.2283

<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: CCP44821.1
RefSeqiNP_216564.2, NC_000962.3
WP_010886138.1, NC_018143.2

3D structure databases

SMRiI6XD69
ModBaseiSearch...

Protein-protein interaction databases

STRINGi83332.Rv2048c

Proteomic databases

PaxDbiI6XD69
PRIDEiI6XD69

Genome annotation databases

GeneIDi888350
KEGGimtu:Rv2048c
PATRICifig|83332.111.peg.2283

Organism-specific databases

TubercuListiRv2048c

Phylogenomic databases

eggNOGiCOG0604, Bacteria
COG3321, Bacteria
OMAiPWRLGMS

Enzyme and pathway databases

UniPathwayiUPA00199
BioCyciMetaCyc:G185E-6251-MONOMER

Family and domain databases

Gene3Di1.10.1200.10, 2 hits
3.10.129.110, 2 hits
3.40.366.10, 2 hits
3.40.47.10, 2 hits
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013154, ADH_N
IPR011032, GroES-like_sf
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 2 hits
PF08240, ADH_N, 1 hit
PF16197, KAsynt_C_assoc, 2 hits
PF00109, ketoacyl-synt, 2 hits
PF02801, Ketoacyl-synt_C, 2 hits
PF08659, KR, 2 hits
PF00550, PP-binding, 2 hits
PF14765, PS-DH, 2 hits
SMARTiView protein in SMART
SM00827, PKS_AT, 2 hits
SM00826, PKS_DH, 2 hits
SM00829, PKS_ER, 2 hits
SM00825, PKS_KS, 2 hits
SM00823, PKS_PP, 2 hits
SUPFAMiSSF47336, SSF47336, 2 hits
SSF50129, SSF50129, 2 hits
SSF51735, SSF51735, 6 hits
SSF52151, SSF52151, 2 hits
SSF53901, SSF53901, 2 hits
SSF55048, SSF55048, 2 hits
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 2 hits
PS50075, CARRIER, 2 hits
PS00012, PHOSPHOPANTETHEINE, 2 hits

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 nameiPKS12_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: I6XD69
Secondary accession number(s): L0TA10
<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: April 7, 2021
This is version 60 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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