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B2HIL7

- MSL7_MYCMM

UniProt

B2HIL7 - MSL7_MYCMM

Protein

Phenolphthiocerol synthesis polyketide synthase type I Pks15/1

Gene

pks15/1

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    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).1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 1 phosphopantetheine covalently.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei211 – 2111For beta-ketoacyl synthase activityCurated
    Active sitei662 – 6621For acyltransferase activityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1530 – 154718NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1719 – 173416NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. Actinobacterium-type cell wall biogenesis Source: UniProtKB
    2. fatty acid biosynthetic process Source: UniProtKB-UniPathway
    3. lipid biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMMAR216594:GJOB-1772-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:pks15/1
    Synonyms:msl7
    Ordered Locus Names:MMAR_1762
    OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
    Taxonomic identifieri216594 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000001190: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. polyketide synthase complex Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111C → A: The pHBA starter unit is not loaded onto Pks15/1 and thus the pHPA intermediate is not produced. 1 Publication
    Mutagenesisi2039 – 20391S → A: The pHBA starter unit is loaded onto Pks15/1, but the pHPA intermediate is not produced. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 21042104Phenolphthiocerol synthesis polyketide synthase type I Pks15/1PRO_0000406361Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2039 – 20391O-(pantetheine 4'-phosphoryl)serineCurated

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi216594.MMAR_1762.

    Structurei

    3D structure databases

    ProteinModelPortaliB2HIL7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2002 – 207675Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 466430Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni571 – 887317AcyltransferaseBy similarityAdd
    BLAST
    Regioni935 – 1095161DehydrataseBy similarityAdd
    BLAST
    Regioni1400 – 1705306EnoylreductaseBy similarityAdd
    BLAST
    Regioni1718 – 1899182Beta-ketoacyl reductase (KR)Add
    BLAST

    Sequence similaritiesi

    Belongs to the beta-ketoacyl-ACP synthases family.Curated
    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3321.
    HOGENOMiHOG000046292.
    KOiK12430.
    OMAiHAHAVES.
    OrthoDBiEOG6W19KW.

    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.
    IPR015083. Polyketide_synth_docking.
    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.
    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]
    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]
    SUPFAMiSSF101173. SSF101173. 1 hit.
    SSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53901. SSF53901. 1 hit.
    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.

    B2HIL7-1 [UniParc]FASTAAdd to Basket

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    MTTSGESADQ QNDKLFRYLK KVAVELDEAR ARLREYEQRA TEPVAVVGIG     50
    CRFPGGADGP EGLWDLVSQG RDAVTEFPND RGWDTEGLFD PDPDAEGKTY 100
    TRWGAFVENA TNFDAGFFGI PPSEVLAMDP QQRLMLEVSW EALEHAGIDP 150
    MSLRGSSTGV FTGIFAPSYG GKDVGALQGY GLTGSPVSVA SGRVAYVLGL 200
    EGPALSVDTA CSSSLVAIHW AMASLRSGEC DMALAGGVTV MGLPSIFVGF 250
    SRQRGLAADG RCKAFAAAAD GTGWGEGAGV LVLERLSDAQ RNGHNVLAVV 300
    RGSAINQDGA SNGLTAPNGL AQQRVIQAAL ANCGLTSADV DVVEAHGTAT 350
    TLGDPIEAEA LLATYGQGRP TDQPLWVGSI KSNMGHTQAA AGVAGVIKMV 400
    QAMRHGLMPA SLHVDEPSKR VDWESGAVSV LAEARDWPDA GRPRRAGVSS 450
    FGISGTNAHV ILEEAPAPEA VPDSESNKGE PSLPVVPWVI SARSAEALTA 500
    QAGRLLAHVQ ADPQSNPVDI GFSLAGRSAF EHRAVVVGAD RQQLLTGLAT 550
    LADGAPGAGV VTGQAGSVGK TAVVFPGQGS QRIGMARELH DQLPVFAEAF 600
    DAVADELDRH LRIPLREVMW GSDAALLDST EFAQPALFAV EVALFAALQR 650
    WGLQPDFVMG HSVGELSAAY VAGVLTLADA AMLVVARGRL MQALPAGGAM 700
    VAVAAAEDEV LPSLTDGVGI AAINAPKSVV ISGAEAAVTA ISDQFAQQGR 750
    RVHRLAVSHA FHSPLMEPML EEFARIAAQV EAREPQIALV SNVTGELASA 800
    DGGFGSAQYW VEHVRRAVRF ADSARQLHTL GVTHFVEVGP GSGLTGSIEQ 850
    SLAPAEAVVV SMLGKDRPEV ASVLTAFGQL FSTGMSVDWP AVFAGSGATR 900
    VDLPTYAFQR RRFWEVPGAD GPADATGLGL GGAEHALLGA VVERPDSGGV 950
    VLTGRLALAD QPWLADHVIG GVVLFPGAGF VELAIRAGDE VGCAVVEELV 1000
    LAAPLVLHPG MGVQVQVIVG AADDSGNRAL SVYSRGDQSE DWLLNAEGML 1050
    GVEAASSGAD LSVWPPEGAE SVDISDGYAQ LADRGYAYGP GFQGLVGVWR 1100
    RDSELFAEVV APSGVAVDKM GMHPVVLDAV LHALGLTAEQ NPDSDETKLP 1150
    FCWRGVSLHA GGAGRVRARL TMSGPDSISV EIADAAGLPV LTVGALVTRA 1200
    MSAAQLRAAV AAAGGGAPDQ GPLDVIWSPI PLSGSGTNGS AQPAVVSWAD 1250
    FCAGGDGGAA GDAGVVVWEP NPAGEDVVGS VYAATHAALE VLQSWFDGDR 1300
    AGTLVVLTHG AVAMPGENVS DLAGAAVWGI VRSAQAENPG RIVLVDADAA 1350
    VEAAELVAVG EPQLVVRSGA AHAARLAPAA PLLAVPADES AWRLAAGGGG 1400
    TLEDLVIEPC PEVQAPLAAG QVRVAVRAVG VNFRDVVAAL GMYPGEAPPL 1450
    GAEGAGVVLE VGPQVSGVAV GDSVMGFLGG AGPLSVVDQQ LITRMPQGWS 1500
    FAQAAAVPVV FLTALFGLQD LAKIQPGESV LIHAGTGGVG MAAVQLARHW 1550
    GVEIFVTASR GKWDTLRAMG FDDDHIGDSR TLDFEEKFLA VTDGRGVDVV 1600
    LDSLAGDFVD ASLRLLVRGG RFLEMGKTDI RDADKIAANY PGVWYRAFDL 1650
    SEAGPVRMQE MLAEVRELFD TAVLHRLPVT TWDVRCAPAA FRFMSQARHI 1700
    GKVVLTMPSA LADGLADATV LITGATGAVG AVLARHMLDA YGVRHLVLAS 1750
    RRGDRAEGAA ELAAELSEAG ANVQVVACDV ADRDAVEAML ARLSGEYPPV 1800
    RGVIHAAGVL DDAVISSLTP ERIDTVLRAK VDAAWNLHEA TLDLDLSMFV 1850
    LCSSIAATVG SPGQGNYSAA NSFLDGLAAH RQAAGLAGIS VAWGLWEQSG 1900
    GMAAHLSSRD LARMSRSGLA PMNPEQAVGL LDAVLAINHP LMVATLLDRP 1950
    ALEARAQAGG LPPLFAGVVR RPRRRQIEDT GDAAQSKSAL AERLNGLSAG 2000
    ERQDALVGLV CLQAAAVLGR PSPEDIDPEA GFQDLGFDSL TAVELRNRLK 2050
    SATGLTLPPT VIFDHPTPTA IAEYVGRQIP DSQATQAEEE KLPESDGEMV 2100
    SVTA 2104
    Length:2,104
    Mass (Da):217,744
    Last modified:June 10, 2008 - v1
    Checksum:i7A33F823206BDCA5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000854 Genomic DNA. Translation: ACC40211.1.
    RefSeqiWP_012393570.1. NC_010612.1.
    YP_001850066.1. NC_010612.1.

    Genome annotation databases

    EnsemblBacteriaiACC40211; ACC40211; MMAR_1762.
    GeneIDi6226021.
    KEGGimmi:MMAR_1762.
    PATRICi18064397. VBIMycMar75906_1883.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000854 Genomic DNA. Translation: ACC40211.1 .
    RefSeqi WP_012393570.1. NC_010612.1.
    YP_001850066.1. NC_010612.1.

    3D structure databases

    ProteinModelPortali B2HIL7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 216594.MMAR_1762.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACC40211 ; ACC40211 ; MMAR_1762 .
    GeneIDi 6226021.
    KEGGi mmi:MMAR_1762.
    PATRICi 18064397. VBIMycMar75906_1883.

    Phylogenomic databases

    eggNOGi COG3321.
    HOGENOMi HOG000046292.
    KOi K12430.
    OMAi HAHAVES.
    OrthoDBi EOG6W19KW.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MMAR216594:GJOB-1772-MONOMER.

    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.
    IPR015083. Polyketide_synth_docking.
    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.
    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 ]
    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 SSF101173. SSF101173. 1 hit.
    SSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53901. SSF53901. 1 hit.
    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

    1. 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.

    Entry informationi

    Entry nameiMSL7_MYCMM
    AccessioniPrimary (citable) accession number: B2HIL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 52 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, Reference proteome

    Documents

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

    External Data

    Dasty 3