UniProt: L7U9K9

Database: UniProt
Entry: L7U9K9_MYXSD

LinkDB:  L7U9K9_MYXSD 
Original site:  L7U9K9_MYXSD

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Ontology (3)   
   GO (3)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (38)   
   InterPro (20)   
   Pfam (8)   
   PROSITE (4)   
   SMART (6)   
Literature (1)   
   PubMed (1)   
All databases (45)   

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ID   L7U9K9_MYXSD            Unreviewed;      1852 AA.
AC   L7U9K9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:AGC45621.1};
GN   OrderedLocusNames=MYSTI_04323 {ECO:0000313|EMBL:AGC45621.1};
OS   Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC45621.1, ECO:0000313|Proteomes:UP000011131};
RN   [1] {ECO:0000313|EMBL:AGC45621.1, ECO:0000313|Proteomes:UP000011131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC   {ECO:0000313|Proteomes:UP000011131};
RX   PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA   Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT   "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT   fruiting myxobacterium.";
RL   Genome Announc. 1:E0010013-E0010013(2013).
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DR   EMBL; CP004025; AGC45621.1; -; Genomic_DNA.
DR   RefSeq; WP_015349881.1; NC_020126.1.
DR   STRING; 1278073.MYSTI_04323; -.
DR   KEGG; msd:MYSTI_04323; -.
DR   PATRIC; fig|1278073.3.peg.4390; -.
DR   eggNOG; COG1028; Bacteria.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_35_3_7; -.
DR   OrthoDB; 5476655at2; -.
DR   Proteomes; UP000011131; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          36..462
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1726..1803
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1852 AA;  199135 MW;  814A64B771EF1615 CRC64;
     MSREFYEKIA NLPPKRLALL ALELNTENEA LKRTRSEPIA IVGTSCRLPG GVESPEDFWR
     LLSNGVDAIR EVPRDRWDAE ALFDPEPGRP GKTYARWGGF IDGIEHFDAG FFGISPREAS
     RMDPQHRMLL ELAWEALERA GQPADQLAGS RTGVFLGVIG SDYARLQAER LGGSLDIYHL
     TGTCLNAAAG RLSYALGLQG PSMAIDTACS SSLVALHTAC QSLRNRDCDL ALAAGVNLML
     SPEGAIALSS SRGLAPDGRC KTFDEAADGF VRAEGVAVVV LKRLSQAQAD GDDILALIAG
     SSVNQDGASS GLMVPNGPAQ ERVIRQALAN AGLSPSQLSF IEAHGTGTSL GDPIELQALA
     QVFGEGRTAE SPLVVGAVKS NIGHLEATAG LAGILKVVLA LRHEAIPPNL HFKRLNPNIA
     IGDAPLVIPT EQRPWPRGEH PRFAGVSAFG LSGTNAHIIL QEAPRPPETP STARGAELLV
     LSARSPEALV ALARRHADWL AEHPETPLRD VCATAALRRA HHEHRLAIAG RTHAEVAEKL
     QALAKGEAVA GGVVGRKAGG ARRRVVFVFP GQGSQWLGMG RRLLAEEPAF RTAMERCAQA
     IRAEAGFDVL EVLAADAEHS RLGEIDVIQP VLFAMEVALA ELWRAWGIEP DAVVGHSMGE
     VAAAQVAGAL SLEDAAAIIC RRSKLLRTVS GQGAMFMVDL TLEEAKEALR GFEDRVSVAV
     SNGVRSTVLS GDPVALEEVT GRLAAREVFF RPVKVDVASH SPQMDPLRPE LLTALEGVRP
     RAASIPMCST VTGAMVDGTS FHARYWVDNL RAPVLFSTAI ERLATEGHDL FIELSPHPIL
     LPAVEQHLRH LGRTGTVVPS LRRDEDERSA MLAALGAIHV TGHGVDLRRQ HPVLSRPVAL
     PTYAWQRESF WVEAPARSRR ARTAGRHPLL GEHVTLAAQP GMHLWQTELS ADSPAYLADH
     LVHGEVVLPG AAYLEMAVAG AVEAWGAKRW MLEDVSFQAL MTVPREEGLP VQLSITPEAE
     GASRFQVFSR PSAEGDWTLH VEGRLRSDDG APVAFSLDQT RTRCTERVEG EAHYQVMGER
     GVDFGPSFRV LEELWRTKGE ALARFELSPS VAAELSTHQV HPVLLDACFQ VINGAAMGAA
     RGETFVPVGL DSLRVHGRPG KSLWGHAVIR RDASGAEGTL EGEVTLLDAE GRVLVEAKGL
     VCRRLKATRR RAVDEIDGWM YAVDWRESPR TLPDASVTNR EPGVWLLFGD PQGFGCKVRT
     LLEARGESCV LVAAGDAYRR VEAGRYEVDL SRPDGFTQLL ESEFGPGKPT CRGVVHLFSL
     DAHPEALEEA QRLGVKSALH LVQALVEASF RDVPRLWLVS GGIHAVNAGD AVSRVEHAPL
     WGLGRVLSVE HSELSCTNVD LQALDDAEAA SFVEELLTPS PEDQLALRGG ARFVARLERL
     EREAAPPADL RADGTYLITG GLGGLGLKLA EWLVSRGARS LALVGRKGAS AEARHVIEKL
     QGAGVQVQVC QADVAVRADV ERVVAELQGV PPLRGLFHAA AVLDDAFLVN LTSERFDKVM
     APKVQGAWNL HAATLGLPLD FFVLFSAAGA LLGSPGQGNY AASNTFLDSL AAWRRGQGLP
     ALSINWGAWG EVGLAAATSN RGDRMALRGI ASMPPDQALE ALGRLLNSTR ARVAVMRFDL
     RQWREFYLTA SRSPFVSRLP LEQAATSTRA APGAFVEKLK AAAQGEQPRL LEAHLREQIG
     QVLRLSPAKI DPQVSLGSLG LDSLMGLEIR NRLEASLGLR LQATLLWRHP TVEGLVGFLV
     ERLQLAPAPK VEQPRNEEAA LEAAIVNNVK QLSDAEAEAL LAEKLAAFGE EN
//

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