UniProtKB - O53901 (PKS5_MYCTU)
Protein
Mycocerosic acid synthase-like polyketide synthase
Gene
pks5
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Polyketide synthase likely involved in the biosynthesis of a polymethyl-branched fatty acid (PMB-FA) that might only be produced during host infection. Is required for the full virulence of M.tuberculosis during host infection.Curated1 Publication
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 185 | Acyl-thioester intermediate; for beta-ketoacyl synthase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 634 | Acyl-ester intermediate; for acyltransferase activityBy similarity | 1 | |
Active sitei | 938 | Proton acceptor; for dehydratase activityBy similarity | 1 | |
Active sitei | 1108 | Proton donor; for dehydratase activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1773 – 1776 | NADPBy similarity | 4 | |
Nucleotide bindingi | 1796 – 1799 | NADPBy similarity | 4 | |
Nucleotide bindingi | 1824 – 1825 | NADPBy similarity | 2 | |
Nucleotide bindingi | 1897 – 1898 | NADPBy similarity | 2 |
GO - Molecular functioni
- oxidoreductase activity Source: UniProtKB-KW
- phosphopantetheine binding Source: InterPro
- transferase activity, transferring acyl groups Source: UniProtKB-KW
GO - Biological processi
- fatty acid biosynthetic process Source: UniProtKB-UniPathway
- pathogenesis Source: MTBBASE
Keywordsi
Molecular function | Acyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase |
Biological process | Fatty acid metabolism, Lipid metabolism, Virulence |
Ligand | NADP |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5715-MONOMER |
Reactomei | R-MTU-9635470 Dimycocersyl phthiocerol biosynthesis |
UniPathwayi | UPA00094 |
Names & Taxonomyi
Protein namesi | Recommended name: Mycocerosic acid synthase-like polyketide synthase1 Publication (EC:2.3.1.-By similarity)Short name: MAS-like PKS1 Publication Alternative name(s): Polyketide synthase Pks5 |
Gene namesi | Name:pks51 PublicationImported Ordered Locus Names:Rv1527cImported, LH57_08370Imported |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv1527c |
Subcellular locationi
- Cell membrane PROSITE-ProRule annotation; Lipid-anchor PROSITE-ProRule annotation
GO - Cellular componenti
- cell wall Source: MTBBASE
- cytosol Source: MTBBASE
- plasma membrane Source: MTBBASE
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
Disruption of this gene causes no major change in the fatty acid and lipid contents of the mutant strain in vitro; the mutant produces all the major methyl-branched fatty acid containing lipids, including DIM, in similar amounts to the wild-type strain. The replication of this mutant is unaffected in mouse bone-marrow macrophages. However, the mutant strain displays severe growth defects in mice, since it multiplies much less extensively than does the parental strain during the acute phase of infection in the lungs and spleen of mice infected via the respiratory route.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 23 | PROSITE-ProRule annotationAdd BLAST | 23 | |
ChainiPRO_0000437078 | 24 – 2108 | Mycocerosic acid synthase-like polyketide synthaseAdd BLAST | 2085 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 24 | N-palmitoyl cysteinePROSITE-ProRule annotation | 1 | |
Lipidationi | 24 | S-diacylglycerol cysteinePROSITE-ProRule annotation | 1 | |
Modified residuei | 2060 | O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation | 1 |
Keywords - PTMi
Lipoprotein, Palmitate, Phosphopantetheine, PhosphoproteinProteomic databases
PaxDbi | O53901 |
PRIDEi | O53901 |
Expressioni
Inductioni
Is expressed in bacteria grown axenically (7H9 medium) and inside macrophages.1 Publication
Interactioni
Subunit structurei
Homodimer.
By similarityProtein-protein interaction databases
STRINGi | 83332.Rv1527c |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2025 – 2101 | CarrierPROSITE-ProRule annotationAdd BLAST | 77 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 14 – 437 | Beta-ketoacyl synthase (KS)By similarityAdd BLAST | 424 | |
Regioni | 438 – 542 | Linker domain (LD)By similarityAdd BLAST | 105 | |
Regioni | 543 – 842 | Acyltransferase (AT)By similarityAdd BLAST | 300 | |
Regioni | 900 – 1184 | Dehydratase (DH)By similarityAdd BLAST | 285 | |
Regioni | 1220 – 1391 | Pseudo beta-ketoacyl reductase (PsiKR)By similarityAdd BLAST | 172 | |
Regioni | 1419 – 1743 | Enoylreductase (ER)By similarityAdd BLAST | 325 | |
Regioni | 1765 – 2004 | Beta-ketoacyl reductase (KR)By similarityAdd BLAST | 240 |
Domaini
Is organized in a condensing KS-AT and a modifying DH-PsiKR-ER-KR region, followed by a flexibly tethered ACP domain.By similarity
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | COG3321 LUCA |
HOGENOMi | HOG000046292 |
KOi | K12433 |
OMAi | MSDNMVI |
PhylomeDBi | O53901 |
Family and domain databases
Gene3Di | 1.10.1200.10, 1 hit 3.10.129.110, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit |
InterProi | View protein in InterPro IPR001227 Ac_transferase_dom_sf IPR036736 ACP-like_sf IPR014043 Acyl_transferase IPR016035 Acyl_Trfase/lysoPLipase IPR013149 ADH_C IPR013154 ADH_N IPR011032 GroES-like_sf IPR032821 KAsynt_C_assoc IPR018201 Ketoacyl_synth_AS IPR014031 Ketoacyl_synth_C IPR014030 Ketoacyl_synth_N IPR016036 Malonyl_transacylase_ACP-bd IPR036291 NAD(P)-bd_dom_sf IPR020801 PKS_acyl_transferase 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 IPR016039 Thiolase-like |
Pfami | View protein in Pfam PF00698 Acyl_transf_1, 1 hit PF08240 ADH_N, 1 hit PF00107 ADH_zinc_N, 1 hit PF16197 KAsynt_C_assoc, 1 hit PF00109 ketoacyl-synt, 1 hit PF02801 Ketoacyl-synt_C, 1 hit PF08659 KR, 1 hit PF00550 PP-binding, 1 hit PF14765 PS-DH, 1 hit |
SMARTi | View protein in SMART SM00827 PKS_AT, 1 hit SM00826 PKS_DH, 1 hit SM00829 PKS_ER, 1 hit SM00825 PKS_KS, 1 hit SM00823 PKS_PP, 1 hit |
SUPFAMi | SSF47336 SSF47336, 1 hit SSF50129 SSF50129, 1 hit SSF51735 SSF51735, 3 hits SSF52151 SSF52151, 1 hit SSF53901 SSF53901, 1 hit SSF55048 SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00606 B_KETOACYL_SYNTHASE, 1 hit PS50075 CARRIER, 1 hit PS51257 PROKAR_LIPOPROTEIN, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
O53901-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGKERTKTVD RTRVTPVAVI GMGCRLPGGI DSPDRLWEAL LRGDDLVTEI
60 70 80 90 100
PADRWDIDEY YDPEPGVPGR TDCKWGAYLD NVGDFDPEFF GIGEKEAIAI
110 120 130 140 150
DPQHRLLLET SWEAMEHGGL TPNQMASRTG VFVGLVHTDY ILVHADNQTF
160 170 180 190 200
EGPYGNTGTN ACFASGRVAY AMGLQGPAIT VDTACSSGLT AIHLACRSLH
210 220 230 240 250
DGESDIALAG GVYVMLEPRR FASGSALGML SATGRCHAFD VSADGFVSGE
260 270 280 290 300
GCVMLALKRL PDALADGDRI LAVIRGTAAN QDGHTVNIAT PSRSAQVAAY
310 320 330 340 350
REALDVAGVD PATVGMVEAH GPGTPVGDPI EYASLAEVYG NDGPCALASV
360 370 380 390 400
KTNFGHTQSA AGALGLMKAV LALQHGVVPQ NLHFTALPDK LAAIETNLFV
410 420 430 440 450
PQEITPWPGA DQETPRRAAV SSYGMTGTNV HAIVEQAPVP APESGAPGDT
460 470 480 490 500
PATPGIDGAL LFALSASSQD ALRQTAARLA DWVDAQGPEL APADLAYTLA
510 520 530 540 550
RRRGHRPVRT AVLAATTAEL TEALREVATG EPPYPPAVGQ DDRGPVWVFS
560 570 580 590 600
GQGSQWAGMG ADLLATEPVF AATIAAIEPL IAAESGFSVT EAMTAPEVVT
610 620 630 640 650
GIDRVQPTLF AMQVALAATM KSYGVAPGAV IGHSLGESAA AVVAGALCLE
660 670 680 690 700
DGVRVICRRS ALMTRIAGAG AMASVELPAQ QVLSELMARG VNDAVVAVVA
710 720 730 740 750
SPQSTVIGGA TQTVRDLVAA WEQRDVLARE VAVDVASHSP QVDPILDELA
760 770 780 790 800
EALAEISPLQ PEIPYYSATS FDPREEPYCD AYYWVDNLRH TVRFAAAVQA
810 820 830 840 850
ALEDGYRVFT ELTPHPLLTH AVDQTARSLD MSAAALAGMR REQPLPHGLR
860 870 880 890 900
ALAGDLYAAG AAVDFAVLYP TGRLINAPLP TWNHRRLLLD DTTRRIAHAN
910 920 930 940 950
TVAVHPLLGS HVRLPEEPER HVWQGEVGTV TQPWLADHQI HGAAALPGAA
960 970 980 990 1000
YCEMALAAAR AVLGEASEVR DIRFEQMLLL DDETPIGVTA TVEAPGVVPL
1010 1020 1030 1040 1050
TVETSHDGRY TRQLAAVLHV VREADDAPDQ PPQKNIAELL ASHPHKVDGA
1060 1070 1080 1090 1100
EVRQWLDKRG HRLGPAFAGL VDAYIAEGAG DTVLAEVNLP GPLRSQVKAY
1110 1120 1130 1140 1150
GVHPVLLDAC FQSVAAHPAV QGMADGGLLL PLGVRRLRSY GSARHARYCC
1160 1170 1180 1190 1200
TTVTACGVGV EADLDVLDEH GAVVLAVRGL QLGTGASQAS ERARVLGERL
1210 1220 1230 1240 1250
LSIEWHEREL PENSHAEPGA WLLISTCDAT DLVAAQLTDA LKVHDAQCTT
1260 1270 1280 1290 1300
MSWPQRADHA AQAARLRDQL GTGGFTGVFV LTAPQTGDPD AESPVRGGEL
1310 1320 1330 1340 1350
VKHVVRIARE IPEITAQEPR LYVLTHNAQA VLSGDRPNLE QGGMRGLLRV
1360 1370 1380 1390 1400
IGAEHPHLKA SYVDVDEQTG AESVARQLLA ASGEDETAWR NDQWYTARLC
1410 1420 1430 1440 1450
PAPLRPEERQ TTVVDHAEAG MRLQIRTPGD LQTLEFAAFD RVPPGPGEIE
1460 1470 1480 1490 1500
VAVTASSINF ADVLVTFGRY QTLDGRQPQL GTDFAGVVSA VGPGVSELKV
1510 1520 1530 1540 1550
GDRVGGMSPN GCWATFVTCD ARLATRLPEG LTDAQAAAVT TASATAWYGL
1560 1570 1580 1590 1600
QDLARIKAGD KVLIHSATGG VGQAAIAIAR AAGAQIYATA GNEKRRDLLR
1610 1620 1630 1640 1650
DMGIEHVYDS RSVEFAEQIR RDTAGYGVDI VLNSVTGAAQ LAGLKLLALG
1660 1670 1680 1690 1700
GRFIEIGKRD IYSNTRLELL PFRRNLAFYG LDLGLMSVSH PAAVRELLST
1710 1720 1730 1740 1750
VYRLTVEGVL PMPQSTHYPL AEAATAIRVM GAAEHTGKLI LDVPHAGRSS
1760 1770 1780 1790 1800
VVLPPEQARV FRSDGSYIIT GGLGGLGLFL AEKMANAGAG RIVLSSRSQP
1810 1820 1830 1840 1850
SQKALETIEL VRAIGSDVVV ECGDIAQPDT ADRLVTAATA TGLPLRGVLH
1860 1870 1880 1890 1900
AAAVVEDATL ANITDELIER DWAPKAYGAW QLHRATADQP LDWFCSFSSA
1910 1920 1930 1940 1950
AALVGSPGQG AYAAANSWLD TFTHWRRAQD LPATSIAWGA WGQIGRAIAF
1960 1970 1980 1990 2000
AEQTGDAIAP EEGAYAFETL LRHNRAYSGY APVIGSPWLT AFAQHSPFAE
2010 2020 2030 2040 2050
KFQSLGQNRS GTSKFLAELV DLPREEWPDR LRRLLSKQVG LILRRTIDTD
2060 2070 2080 2090 2100
RLLSEYGLDS LSSQELRARV EAETGIRISA TEINTTVRGL ADLMCDKLAA
DRDAPAPA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44291.1 CP009480 Genomic DNA Translation: AIR14281.1 |
RefSeqi | NP_216043.1, NC_000962.3 WP_003913253.1, NZ_NVQJ01000004.1 |
Genome annotation databases
EnsemblBacteriai | AIR14281; AIR14281; LH57_08370 CCP44291; CCP44291; Rv1527c |
GeneIDi | 886442 |
KEGGi | mtu:Rv1527c mtv:RVBD_1527c |
PATRICi | fig|83332.111.peg.1704 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP44291.1 CP009480 Genomic DNA Translation: AIR14281.1 |
RefSeqi | NP_216043.1, NC_000962.3 WP_003913253.1, NZ_NVQJ01000004.1 |
3D structure databases
SMRi | O53901 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv1527c |
Proteomic databases
PaxDbi | O53901 |
PRIDEi | O53901 |
Genome annotation databases
EnsemblBacteriai | AIR14281; AIR14281; LH57_08370 CCP44291; CCP44291; Rv1527c |
GeneIDi | 886442 |
KEGGi | mtu:Rv1527c mtv:RVBD_1527c |
PATRICi | fig|83332.111.peg.1704 |
Organism-specific databases
TubercuListi | Rv1527c |
Phylogenomic databases
eggNOGi | COG3321 LUCA |
HOGENOMi | HOG000046292 |
KOi | K12433 |
OMAi | MSDNMVI |
PhylomeDBi | O53901 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
BioCyci | MTBH37RV:G185E-5715-MONOMER |
Reactomei | R-MTU-9635470 Dimycocersyl phthiocerol biosynthesis |
Family and domain databases
Gene3Di | 1.10.1200.10, 1 hit 3.10.129.110, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit |
InterProi | View protein in InterPro IPR001227 Ac_transferase_dom_sf IPR036736 ACP-like_sf IPR014043 Acyl_transferase IPR016035 Acyl_Trfase/lysoPLipase IPR013149 ADH_C IPR013154 ADH_N IPR011032 GroES-like_sf IPR032821 KAsynt_C_assoc IPR018201 Ketoacyl_synth_AS IPR014031 Ketoacyl_synth_C IPR014030 Ketoacyl_synth_N IPR016036 Malonyl_transacylase_ACP-bd IPR036291 NAD(P)-bd_dom_sf IPR020801 PKS_acyl_transferase 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 IPR016039 Thiolase-like |
Pfami | View protein in Pfam PF00698 Acyl_transf_1, 1 hit PF08240 ADH_N, 1 hit PF00107 ADH_zinc_N, 1 hit PF16197 KAsynt_C_assoc, 1 hit PF00109 ketoacyl-synt, 1 hit PF02801 Ketoacyl-synt_C, 1 hit PF08659 KR, 1 hit PF00550 PP-binding, 1 hit PF14765 PS-DH, 1 hit |
SMARTi | View protein in SMART SM00827 PKS_AT, 1 hit SM00826 PKS_DH, 1 hit SM00829 PKS_ER, 1 hit SM00825 PKS_KS, 1 hit SM00823 PKS_PP, 1 hit |
SUPFAMi | SSF47336 SSF47336, 1 hit SSF50129 SSF50129, 1 hit SSF51735 SSF51735, 3 hits SSF52151 SSF52151, 1 hit SSF53901 SSF53901, 1 hit SSF55048 SSF55048, 1 hit |
PROSITEi | View protein in PROSITE PS00606 B_KETOACYL_SYNTHASE, 1 hit PS50075 CARRIER, 1 hit PS51257 PROKAR_LIPOPROTEIN, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PKS5_MYCTU | |
Accessioni | O53901Primary (citable) accession number: O53901 Secondary accession number(s): F2GEH5, I6XBP9, L0T6X5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 7, 2016 |
Last sequence update: | August 1, 1998 | |
Last modified: | October 16, 2019 | |
This is version 146 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways