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Q7TXL8

- PPSC_MYCBO

UniProt

Q7TXL8 - PPSC_MYCBO

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Protein
Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsC
Gene
ppsC, Mb2958
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the elongation of either C22-24 fatty acids or p-hydroxyphenylalkanoic acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol and phenolphthiocerol derivatives, respectively.1 Publication

Catalytic activityi

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Cofactori

Binds 1 phosphopantetheines covalently By similarity.
NADP By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei210 – 2101For beta-ketoacyl synthase activity By similarity
Active sitei660 – 6601For malonyltransferase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1803 – 184846NADP By similarity
Add
BLAST

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
  2. oxidoreductase activity Source: UniProtKB-KW
  3. phosphopantetheine binding Source: InterPro
  4. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. Actinobacterium-type cell wall biogenesis Source: UniProtKB
  2. fatty acid biosynthetic process Source: UniProtKB-UniPathway
  3. phenolic phthiocerol biosynthetic process Source: UniProtKB
  4. phthiocerol biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsC
Alternative name(s):
Beta-ketoacyl-acyl-carrier-protein synthase I (EC:2.3.1.41)
Gene namesi
Name:ppsC
Ordered Locus Names:Mb2958
OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Taxonomic identifieri233413 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001419: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. polyketide synthase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells lacking this genes abolish the production of phenolphthiocerol derivative (mycoside B) and phthiocerol dimycocerosates (DIM) on the cell envelope.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21882188Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsC
PRO_0000406947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2105 – 21051O-(pantetheine 4'-phosphoryl)serine Reviewed prediction

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

STRINGi233413.Mb2958.

Structurei

3D structure databases

ProteinModelPortaliQ7TXL8.
SMRiQ7TXL8. Positions 1571-1753.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2074 – 214269Acyl carrier
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 465429Beta-ketoacyl synthase By similarity
Add
BLAST
Regioni572 – 890319Acyltransferase By similarity
Add
BLAST
Regioni928 – 1093166Dehydratase By similarity
Add
BLAST
Regioni1467 – 1778312Enoylreductase By similarity
Add
BLAST
Regioni1802 – 1981180Beta-ketoacyl reductase By similarity
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3321.
HOGENOMiHOG000046292.
KOiK12442.
OMAiWCSESEG.
OrthoDBiEOG6QP0WP.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR006162. PPantetheine_attach_site.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TXL8-1 [UniParc]FASTAAdd to Basket

« Hide

MTAATPDRRA IITEALHKID DLTARLEIAE KSSSEPIAVI GMGCRFPGGV     50
NNPEQFWDLL CAGRSGIVRV PAQRWDADAY YCDDHTVPGT ICSTEGGFLT 100
SWQPDEFDAE FFSISPREAA AMDPQQRLLI EVAWEALEDA GVPQHTIRGT 150
QTSVFVGVTA YDYMLTLAGR LRPVDLDAYI PTGNSANFAA GRLAYILGAR 200
GPAVVIDTAC SSSLVAVHLA CQSLRGRESD MALVGGTNLL LSPGPSIACS 250
RWGMLSPEGR CKTFDASADG YVRGEGAAVV VLKRLDDAVR DGNRILAVVR 300
GSAVNQDGAS SGVTVPNGPA QQALLAKALT SSKLTAADID YVEAHGTGTP 350
LGDPIELDSL SKVFSDRAGS DQLVIGSVKT NLGHLEAAAG VAGLMKAVLA 400
VHNGYIPRHL NFHQLTPHAS EAASRLRIAA DGIDWPTTGR PRRAGVSSFG 450
VSGTNAHVVI EQAPDPMAAA GTEPQRGPVP AVSTLVVFGK TAPRVAATAS 500
VLADWLDGPG AAVPLADVAH TLNHHRARQT RFGTVAAVDR RQAVIGLRAL 550
AAGQSAPGVV APREGSIGGG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAI 600
AELEPEFVAQ GGFSLRDVIA GGKELVGIEQ IQLGLIGMQL ALTALWRSYG 650
VTPDAVIGHS MGEVAAAVVA GALTPAQGLR VTAVRSRLMA PLSGQGTMAL 700
LELDAEATEA LIADYPEVSL GIYASPRQTV ISGPPLLIDE LIDKVRQQNG 750
FATRVNIEVA PHNPAMDALQ PAMRSELADL TPQPPTIPII STTYADLGIS 800
LGSGPRFDAE HWATNMRNPV RFHQAIAHAG ADHHTFIEIS AHPLLTHSIS 850
DTLRASYDVD NYLSIGTLQR DAHDTLEFHT NLNTTHTTHP PQTPHPPEPH 900
PVLPTTPWQH TQHWITATSA AYHRPDTHPL LGVGVTDPTN GTRVWESELD 950
PDLLWLADHV IDDLVVLPGA AYAEIALAAA TDTFAVEQDQ PWMISELDLR 1000
QMLHVTPGTV LVTTLTGDEQ RCQVEIRTRS GSSGWTTHAT ATVARAEPLA 1050
PLDHEGQRRE VTTADLEDQL DPDDLYQRLR GAGQQHGPAF QGIVGLAVTQ 1100
AGVARAQVRL PASARTGSRE FMLHPVMMDI ALQTLGATRT ATDLAGGQDA 1150
RQGPSSNSAL VVPVRFAGVH VYGDITRGVR AVGSLAAAGD RLVGEVVLTD 1200
ANGQPLLVVD EVEMAVLGSG SGATELTNRL FMLEWEPAPL EKTAEATGAL 1250
LLIGDPAAGD PLLPALQSSL RDRITDLELA SAADEATLRA AISRTSWDGI 1300
VVVCPPRAND ESMPDEAQLE LARTRTLLVA SVVETVTRMG ARKSPRLWIV 1350
TRGAAQFDAG ESVTLAQTGL RGIARVLTFE HSELNTTLVD IEPDGTGSLA 1400
ALAEELLAGS EADEVALRDG QRYVNRLVPA PTTTSGDLAA EARHQVVNLD 1450
SSGASRAAVR LQIDQPGRLD ALNVHEVKRG RPQGDQVEVR VVAAGLNFSD 1500
VLKAMGVYPG LDGAAPVIGG ECVGYVTAIG DEVDGVEVGQ RVIAFGPGTF 1550
GTHLGTIADL VVPIPDTLAD NEAATFGVAY LTAWHSLCEV GRLSPGERVL 1600
IHSATGGVGM AAVSIAKMIG ARIYTTAGSD AKREMLSRLG VEYVGDSRSV 1650
DFADEILELT DGYGVDVVLN SLAGEAIQRG VQILAPGGRF IELGKKDVYA 1700
DASLGLAALA KSASFSVVDL DLNLKLQPAR YRQLLQHILQ HVADGKLEVL 1750
PVTAFSLHDA ADAFRLMASG KHTGKIVISI PQHGSIEAIA APPPLPLVSR 1800
DGGYLIVGGM GGLGFVVARW LAEQGAGLIV LNGRSAPSDE VAAAIAELNA 1850
SGSRIEVITG DITEPDTAER LVRAVEDAGF RLAGVVHSAM VLADEIVLNM 1900
TDSAARRVFA PKVTGSWRLH VATAARDVDW WLTFSSAAAL LGTPGQGAYA 1950
AANSWVDGLV AHRRSAGLPA VGINWGPWAD VGRAQFFKDL GVEMINAEQG 2000
LAAMQAVLTA DRGRTGVFSL DARQWFQSFP AVAGSSLFAK LHDSAARKSG 2050
QRRGGGAIRA QLDALDAAER PGHLASAIAD EIRAVLRSGD PIDHHRPLET 2100
LGLDSLMGLE LRNRLEASLG ITLPVALVWA YPTISDLATA LCERMDYATP 2150
AAAQEISDTE PELSDEEMDL LADLVDASEL EAATRGES 2188
Length:2,188
Mass (Da):230,622
Last modified:October 1, 2003 - v1
Checksum:i3C431C011F01F1A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248333 Genomic DNA. Translation: CDO44225.1.
RefSeqiNP_856603.1. NC_002945.3.

Genome annotation databases

EnsemblBacteriaiCAD96645; CAD96645; Mb2958.
GeneIDi1092148.
KEGGimbo:Mb2958.
PATRICi18008228. VBIMycBov88188_3246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248333 Genomic DNA. Translation: CDO44225.1 .
RefSeqi NP_856603.1. NC_002945.3.

3D structure databases

ProteinModelPortali Q7TXL8.
SMRi Q7TXL8. Positions 1571-1753.
ModBasei Search...

Protein-protein interaction databases

STRINGi 233413.Mb2958.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD96645 ; CAD96645 ; Mb2958 .
GeneIDi 1092148.
KEGGi mbo:Mb2958.
PATRICi 18008228. VBIMycBov88188_3246.

Phylogenomic databases

eggNOGi COG3321.
HOGENOMi HOG000046292.
KOi K12442.
OMAi WCSESEG.
OrthoDBi EOG6QP0WP.

Enzyme and pathway databases

UniPathwayi UPA00094 .

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProi IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR006162. PPantetheine_attach_site.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view ]
SMARTi SM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-935 / AF2122/97.
  2. "Gene knockout reveals a novel gene cluster for the synthesis of a class of cell wall lipids unique to pathogenic mycobacteria."
    Azad A.K., Sirakova T.D., Fernandes N.D., Kolattukudy P.E.
    J. Biol. Chem. 272:16741-16745(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE PHTHIOCEROL AND PHENOLPHTHIOCEROL BIOSYNTHESIS, DISRUPTION PHENOTYPE.
    Strain: ATCC BAA-935 / AF2122/97.

Entry informationi

Entry nameiPPSC_MYCBO
AccessioniPrimary (citable) accession number: Q7TXL8
Secondary accession number(s): X2BMJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi