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B2HIL7

- MSL7_MYCMM

UniProt

B2HIL7 - MSL7_MYCMM

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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

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

pantetheine 4'-phosphateBy similarityNote: 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
Complete GO annotation...

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
Complete GO annotation...

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

« Hide

        10         20         30         40         50
MTTSGESADQ QNDKLFRYLK KVAVELDEAR ARLREYEQRA TEPVAVVGIG
60 70 80 90 100
CRFPGGADGP EGLWDLVSQG RDAVTEFPND RGWDTEGLFD PDPDAEGKTY
110 120 130 140 150
TRWGAFVENA TNFDAGFFGI PPSEVLAMDP QQRLMLEVSW EALEHAGIDP
160 170 180 190 200
MSLRGSSTGV FTGIFAPSYG GKDVGALQGY GLTGSPVSVA SGRVAYVLGL
210 220 230 240 250
EGPALSVDTA CSSSLVAIHW AMASLRSGEC DMALAGGVTV MGLPSIFVGF
260 270 280 290 300
SRQRGLAADG RCKAFAAAAD GTGWGEGAGV LVLERLSDAQ RNGHNVLAVV
310 320 330 340 350
RGSAINQDGA SNGLTAPNGL AQQRVIQAAL ANCGLTSADV DVVEAHGTAT
360 370 380 390 400
TLGDPIEAEA LLATYGQGRP TDQPLWVGSI KSNMGHTQAA AGVAGVIKMV
410 420 430 440 450
QAMRHGLMPA SLHVDEPSKR VDWESGAVSV LAEARDWPDA GRPRRAGVSS
460 470 480 490 500
FGISGTNAHV ILEEAPAPEA VPDSESNKGE PSLPVVPWVI SARSAEALTA
510 520 530 540 550
QAGRLLAHVQ ADPQSNPVDI GFSLAGRSAF EHRAVVVGAD RQQLLTGLAT
560 570 580 590 600
LADGAPGAGV VTGQAGSVGK TAVVFPGQGS QRIGMARELH DQLPVFAEAF
610 620 630 640 650
DAVADELDRH LRIPLREVMW GSDAALLDST EFAQPALFAV EVALFAALQR
660 670 680 690 700
WGLQPDFVMG HSVGELSAAY VAGVLTLADA AMLVVARGRL MQALPAGGAM
710 720 730 740 750
VAVAAAEDEV LPSLTDGVGI AAINAPKSVV ISGAEAAVTA ISDQFAQQGR
760 770 780 790 800
RVHRLAVSHA FHSPLMEPML EEFARIAAQV EAREPQIALV SNVTGELASA
810 820 830 840 850
DGGFGSAQYW VEHVRRAVRF ADSARQLHTL GVTHFVEVGP GSGLTGSIEQ
860 870 880 890 900
SLAPAEAVVV SMLGKDRPEV ASVLTAFGQL FSTGMSVDWP AVFAGSGATR
910 920 930 940 950
VDLPTYAFQR RRFWEVPGAD GPADATGLGL GGAEHALLGA VVERPDSGGV
960 970 980 990 1000
VLTGRLALAD QPWLADHVIG GVVLFPGAGF VELAIRAGDE VGCAVVEELV
1010 1020 1030 1040 1050
LAAPLVLHPG MGVQVQVIVG AADDSGNRAL SVYSRGDQSE DWLLNAEGML
1060 1070 1080 1090 1100
GVEAASSGAD LSVWPPEGAE SVDISDGYAQ LADRGYAYGP GFQGLVGVWR
1110 1120 1130 1140 1150
RDSELFAEVV APSGVAVDKM GMHPVVLDAV LHALGLTAEQ NPDSDETKLP
1160 1170 1180 1190 1200
FCWRGVSLHA GGAGRVRARL TMSGPDSISV EIADAAGLPV LTVGALVTRA
1210 1220 1230 1240 1250
MSAAQLRAAV AAAGGGAPDQ GPLDVIWSPI PLSGSGTNGS AQPAVVSWAD
1260 1270 1280 1290 1300
FCAGGDGGAA GDAGVVVWEP NPAGEDVVGS VYAATHAALE VLQSWFDGDR
1310 1320 1330 1340 1350
AGTLVVLTHG AVAMPGENVS DLAGAAVWGI VRSAQAENPG RIVLVDADAA
1360 1370 1380 1390 1400
VEAAELVAVG EPQLVVRSGA AHAARLAPAA PLLAVPADES AWRLAAGGGG
1410 1420 1430 1440 1450
TLEDLVIEPC PEVQAPLAAG QVRVAVRAVG VNFRDVVAAL GMYPGEAPPL
1460 1470 1480 1490 1500
GAEGAGVVLE VGPQVSGVAV GDSVMGFLGG AGPLSVVDQQ LITRMPQGWS
1510 1520 1530 1540 1550
FAQAAAVPVV FLTALFGLQD LAKIQPGESV LIHAGTGGVG MAAVQLARHW
1560 1570 1580 1590 1600
GVEIFVTASR GKWDTLRAMG FDDDHIGDSR TLDFEEKFLA VTDGRGVDVV
1610 1620 1630 1640 1650
LDSLAGDFVD ASLRLLVRGG RFLEMGKTDI RDADKIAANY PGVWYRAFDL
1660 1670 1680 1690 1700
SEAGPVRMQE MLAEVRELFD TAVLHRLPVT TWDVRCAPAA FRFMSQARHI
1710 1720 1730 1740 1750
GKVVLTMPSA LADGLADATV LITGATGAVG AVLARHMLDA YGVRHLVLAS
1760 1770 1780 1790 1800
RRGDRAEGAA ELAAELSEAG ANVQVVACDV ADRDAVEAML ARLSGEYPPV
1810 1820 1830 1840 1850
RGVIHAAGVL DDAVISSLTP ERIDTVLRAK VDAAWNLHEA TLDLDLSMFV
1860 1870 1880 1890 1900
LCSSIAATVG SPGQGNYSAA NSFLDGLAAH RQAAGLAGIS VAWGLWEQSG
1910 1920 1930 1940 1950
GMAAHLSSRD LARMSRSGLA PMNPEQAVGL LDAVLAINHP LMVATLLDRP
1960 1970 1980 1990 2000
ALEARAQAGG LPPLFAGVVR RPRRRQIEDT GDAAQSKSAL AERLNGLSAG
2010 2020 2030 2040 2050
ERQDALVGLV CLQAAAVLGR PSPEDIDPEA GFQDLGFDSL TAVELRNRLK
2060 2070 2080 2090 2100
SATGLTLPPT VIFDHPTPTA IAEYVGRQIP DSQATQAEEE KLPESDGEMV

SVTA
Length:2,104
Mass (Da):217,744
Last modified:June 10, 2008 - v1
Checksum:i7A33F823206BDCA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40211.1.
RefSeqiYP_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:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40211.1 .
RefSeqi 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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 54 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