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B2HIL7 (MSL7_MYCMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phenolphthiocerol synthesis polyketide synthase type I Pks15/1
Alternative name(s):
Beta-ketoacyl-acyl-carrier-protein synthase I
EC=2.3.1.41
Gene names
Name:pks15/1
Synonyms:msl7
Ordered Locus Names:MMAR_1762
OrganismMycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]
Taxonomic identifier216594 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length2104 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the elongation by iterative transfer of p-hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-hydroxyphenylalkanoate (pHPA) intermediates during phenolphthiocerol (PPOL) biosynthesis. PPOL is an important intermediate in the biosynthesis of phenolic glycolipid (mycosid B). Ref.2

Catalytic activity

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

Cofactor

Binds 1 phosphopantetheine covalently By similarity.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21042104Phenolphthiocerol synthesis polyketide synthase type I Pks15/1
PRO_0000406361

Regions

Domain2002 – 207675Acyl carrier
Nucleotide binding1530 – 154718NADP By similarity
Nucleotide binding1719 – 173416NADP By similarity
Region37 – 466430Beta-ketoacyl synthase By similarity
Region571 – 887317Acyltransferase By similarity
Region935 – 1095161Dehydratase By similarity
Region1400 – 1705306Enoylreductase By similarity
Region1718 – 1899182Beta-ketoacyl reductase (KR)

Sites

Active site2111For beta-ketoacyl synthase activity Probable
Active site6621For acyltransferase activity By similarity

Amino acid modifications

Modified residue20391O-(pantetheine 4'-phosphoryl)serine Probable

Experimental info

Mutagenesis2111C → A: The pHBA starter unit is not loaded onto Pks15/1 and thus the pHPA intermediate is not produced. Ref.2
Mutagenesis20391S → A: The pHBA starter unit is loaded onto Pks15/1, but the pHPA intermediate is not produced. Ref.2

Sequences

Sequence LengthMass (Da)Tools
B2HIL7 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 7A33F823206BDCA5

FASTA2,104217,744
        10         20         30         40         50         60 
MTTSGESADQ QNDKLFRYLK KVAVELDEAR ARLREYEQRA TEPVAVVGIG CRFPGGADGP 

        70         80         90        100        110        120 
EGLWDLVSQG RDAVTEFPND RGWDTEGLFD PDPDAEGKTY TRWGAFVENA TNFDAGFFGI 

       130        140        150        160        170        180 
PPSEVLAMDP QQRLMLEVSW EALEHAGIDP MSLRGSSTGV FTGIFAPSYG GKDVGALQGY 

       190        200        210        220        230        240 
GLTGSPVSVA SGRVAYVLGL EGPALSVDTA CSSSLVAIHW AMASLRSGEC DMALAGGVTV 

       250        260        270        280        290        300 
MGLPSIFVGF SRQRGLAADG RCKAFAAAAD GTGWGEGAGV LVLERLSDAQ RNGHNVLAVV 

       310        320        330        340        350        360 
RGSAINQDGA SNGLTAPNGL AQQRVIQAAL ANCGLTSADV DVVEAHGTAT TLGDPIEAEA 

       370        380        390        400        410        420 
LLATYGQGRP TDQPLWVGSI KSNMGHTQAA AGVAGVIKMV QAMRHGLMPA SLHVDEPSKR 

       430        440        450        460        470        480 
VDWESGAVSV LAEARDWPDA GRPRRAGVSS FGISGTNAHV ILEEAPAPEA VPDSESNKGE 

       490        500        510        520        530        540 
PSLPVVPWVI SARSAEALTA QAGRLLAHVQ ADPQSNPVDI GFSLAGRSAF EHRAVVVGAD 

       550        560        570        580        590        600 
RQQLLTGLAT LADGAPGAGV VTGQAGSVGK TAVVFPGQGS QRIGMARELH DQLPVFAEAF 

       610        620        630        640        650        660 
DAVADELDRH LRIPLREVMW GSDAALLDST EFAQPALFAV EVALFAALQR WGLQPDFVMG 

       670        680        690        700        710        720 
HSVGELSAAY VAGVLTLADA AMLVVARGRL MQALPAGGAM VAVAAAEDEV LPSLTDGVGI 

       730        740        750        760        770        780 
AAINAPKSVV ISGAEAAVTA ISDQFAQQGR RVHRLAVSHA FHSPLMEPML EEFARIAAQV 

       790        800        810        820        830        840 
EAREPQIALV SNVTGELASA DGGFGSAQYW VEHVRRAVRF ADSARQLHTL GVTHFVEVGP 

       850        860        870        880        890        900 
GSGLTGSIEQ SLAPAEAVVV SMLGKDRPEV ASVLTAFGQL FSTGMSVDWP AVFAGSGATR 

       910        920        930        940        950        960 
VDLPTYAFQR RRFWEVPGAD GPADATGLGL GGAEHALLGA VVERPDSGGV VLTGRLALAD 

       970        980        990       1000       1010       1020 
QPWLADHVIG GVVLFPGAGF VELAIRAGDE VGCAVVEELV LAAPLVLHPG MGVQVQVIVG 

      1030       1040       1050       1060       1070       1080 
AADDSGNRAL SVYSRGDQSE DWLLNAEGML GVEAASSGAD LSVWPPEGAE SVDISDGYAQ 

      1090       1100       1110       1120       1130       1140 
LADRGYAYGP GFQGLVGVWR RDSELFAEVV APSGVAVDKM GMHPVVLDAV LHALGLTAEQ 

      1150       1160       1170       1180       1190       1200 
NPDSDETKLP FCWRGVSLHA GGAGRVRARL TMSGPDSISV EIADAAGLPV LTVGALVTRA 

      1210       1220       1230       1240       1250       1260 
MSAAQLRAAV AAAGGGAPDQ GPLDVIWSPI PLSGSGTNGS AQPAVVSWAD FCAGGDGGAA 

      1270       1280       1290       1300       1310       1320 
GDAGVVVWEP NPAGEDVVGS VYAATHAALE VLQSWFDGDR AGTLVVLTHG AVAMPGENVS 

      1330       1340       1350       1360       1370       1380 
DLAGAAVWGI VRSAQAENPG RIVLVDADAA VEAAELVAVG EPQLVVRSGA AHAARLAPAA 

      1390       1400       1410       1420       1430       1440 
PLLAVPADES AWRLAAGGGG TLEDLVIEPC PEVQAPLAAG QVRVAVRAVG VNFRDVVAAL 

      1450       1460       1470       1480       1490       1500 
GMYPGEAPPL GAEGAGVVLE VGPQVSGVAV GDSVMGFLGG AGPLSVVDQQ LITRMPQGWS 

      1510       1520       1530       1540       1550       1560 
FAQAAAVPVV FLTALFGLQD LAKIQPGESV LIHAGTGGVG MAAVQLARHW GVEIFVTASR 

      1570       1580       1590       1600       1610       1620 
GKWDTLRAMG FDDDHIGDSR TLDFEEKFLA VTDGRGVDVV LDSLAGDFVD ASLRLLVRGG 

      1630       1640       1650       1660       1670       1680 
RFLEMGKTDI RDADKIAANY PGVWYRAFDL SEAGPVRMQE MLAEVRELFD TAVLHRLPVT 

      1690       1700       1710       1720       1730       1740 
TWDVRCAPAA FRFMSQARHI GKVVLTMPSA LADGLADATV LITGATGAVG AVLARHMLDA 

      1750       1760       1770       1780       1790       1800 
YGVRHLVLAS RRGDRAEGAA ELAAELSEAG ANVQVVACDV ADRDAVEAML ARLSGEYPPV 

      1810       1820       1830       1840       1850       1860 
RGVIHAAGVL DDAVISSLTP ERIDTVLRAK VDAAWNLHEA TLDLDLSMFV LCSSIAATVG 

      1870       1880       1890       1900       1910       1920 
SPGQGNYSAA NSFLDGLAAH RQAAGLAGIS VAWGLWEQSG GMAAHLSSRD LARMSRSGLA 

      1930       1940       1950       1960       1970       1980 
PMNPEQAVGL LDAVLAINHP LMVATLLDRP ALEARAQAGG LPPLFAGVVR RPRRRQIEDT 

      1990       2000       2010       2020       2030       2040 
GDAAQSKSAL AERLNGLSAG ERQDALVGLV CLQAAAVLGR PSPEDIDPEA GFQDLGFDSL 

      2050       2060       2070       2080       2090       2100 
TAVELRNRLK SATGLTLPPT VIFDHPTPTA IAEYVGRQIP DSQATQAEEE KLPESDGEMV 


SVTA 

« Hide

References

« Hide 'large scale' references
[1]"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis."
Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. expand/collapse author list , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.
Genome Res. 18:729-741(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-535 / M.
[2]"Cooperation between a coenzyme A-independent stand-alone initiation module and an iterative type I polyketide synthase during synthesis of mycobacterial phenolic glycolipids."
He W., Soll C.E., Chavadi S.S., Zhang G., Warren J.D., Quadri L.E.
J. Am. Chem. Soc. 131:16744-16750(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A POLYKETIDE SYNTHASE, MUTAGENESIS OF CYS-211 AND SER-2039.
Strain: ATCC BAA-535 / M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000854 Genomic DNA. Translation: ACC40211.1.
RefSeqYP_001850066.1. NC_010612.1.

3D structure databases

ProteinModelPortalB2HIL7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216594.MMAR_1762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACC40211; ACC40211; MMAR_1762.
GeneID6226021.
KEGGmmi:MMAR_1762.
PATRIC18064397. VBIMycMar75906_1883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3321.
HOGENOMHOG000046292.
KOK12430.
OMAHAHAVES.
OrthoDBEOG6W19KW.

Enzyme and pathway databases

BioCycMMAR216594:GJOB-1772-MONOMER.
UniPathwayUPA00094.

Family and domain databases

Gene3D1.10.1200.10. 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.
InterProIPR001227. 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.
IPR015083. Polyketide_synth_docking.
IPR006162. PPantetheine_attach_site.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF08990. Docking. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTSM00827. 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]
SUPFAMSSF101173. SSF101173. 1 hit.
SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 1 hit.
SSF55048. SSF55048. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMSL7_MYCMM
AccessionPrimary (citable) accession number: B2HIL7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways