ID K2QVA6_MACPH Unreviewed; 2275 AA.
AC K2QVA6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:EKG13586.1};
DE Flags: Fragment;
GN ORFNames=MPH_09266 {ECO:0000313|EMBL:EKG13586.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG13586.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG13586.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG13586.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG13586.1}.
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DR EMBL; AHHD01000405; EKG13586.1; -; Genomic_DNA.
DR STRING; 1126212.K2QVA6; -.
DR VEuPathDB; FungiDB:MPH_09266; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_2_1; -.
DR InParanoid; K2QVA6; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
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 GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 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; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR013217; Methyltransf_12.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..796
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1623..1702
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1729..1806
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 2275
FT /evidence="ECO:0000313|EMBL:EKG13586.1"
SQ SEQUENCE 2275 AA; 246080 MW; 830440C281A33981 CRC64;
MISTAIFCPQ SKGTPKPYLD SLRLYLTGNH RLQPIHSVLK NLGDDWSTLV SEFEEFGGLP
QGPRWTKSIR DWIVDGHAAP LADAMAGTVC LPLLVVMQVC QYFQFLEVKG MRHAEMIAGL
KGGAHGYCGG ILPAVAVACA GDEDEIIQQA CVALRVAFAI GVASDFGDDD ESIIGPSTIV
ARIKRPGQLE ELLAKFPGTY HSANTDARTV SIVGPVLTLK ALSDHAKTMG LFVQGIHLRG
KVHNPENREL ANRIGLFCEN HPGFRLPRAD RLRVPLRSNI TGQPLVGDES LTIDCVQTIL
AARCEWHTVM KGIAKDLQAS HVVSHTFASF GIGDVIPMAP FNAAGLRINK LDVRSIVEAS
LPQSIPQANY EYPDDAVAII GVGCRVPGAN SLEELWELLA RGESTCQEVP SSRIDIPGNF
RAKLDGGMNK QKFYGNFIDN VDAFDHTFFH VSPKEAKHMD PQQRILLEVA YQAMESSGYM
ATHKREAGDP VGFFIATSFI EYLENSTCHP PTAFTCTGTL RAFLCGRISH YFGWTGPSEL
IDTACSASLV AINRACRAVR TGECPIALAG GINIMAGCQN FLNLSKAGFL SETGQCKPFD
AGADGYCRSE GVGLIVLKSL KQALEDADPI IGVVSGVATN QGGLSASLTV PSEDAQVALF
QNVLRQSKLR PDQITYAEAH GTGTQAGDPV EIASLRKVFG GAQRPNHLYI GSLKGNIGHL
ESAAGVAGLL KVLAMLKHRV IPQQASFSKI NPKFPPLGPD RLAIAQTSQP WQHEFKAALV
NSYGAAGSNA AMICCQPPAR QGSNHQSYAA AYPLRVGANS EKSLTAILAA LKRHLLQPGA
AVTLADLSFT LSERRKKHEF QWAATASSIG EAVSALEAKN TPFERMSAPE RHVVLLFSGQ
SKQNVLLNKQ FYASQPLLRY HIEQCSKTLF QYGFPPIVPA IFQEEAIADP VVLQCATFAL
QYSCAKSWID SGLKVDAIIG HSFGELTGLV ASGALSLGDG LLLVATRAML MKTKWGAERG
TMLAIHADRN TVEKIALMVP GVEVACYNAP SSQVLVGTTA GIDEVERLLS SNYSAIKCKR
LNVSHGFHSR FTQPLLPELQ ELTGKLSFKI PRIPLETCTE NPGAITTPNY LVHHTRMPVY
FTDAIRRVER KFGACVFLEA GTDTPITAMA KHAVANPTRH VFQPLSSHND RNGLASATVA
LWTQGLSVSY WAFVASAGME VPLPQQVWLP PYQFDRSTSF WLPFVDRSHE AQNSEKAPIM
VQSKLEEPRF LVSSLSAPDG LYVVNTGAER FTSLVSGHAV RGQPLCPASL YMECATMAVQ
LAGNDLQGKS LLFENITYSA PLGNGISKDT MLSLERSDLP GSWQFSMSSS MNTSASQKKP
EIHATGRLSI GTQKSDQNQL VERLVADRVS TLKTRSDVDN LSAARAYSLF SRVVRYSDMF
RGISNIVMAT NEAIAAVNVP PSTAEPSQST ATKRCETVAL DTFLQVLGLL INSSTHADED
CVCVATGLDS ATISTSADFN AVREYNVYTT FTRSSQGRFV GDVFVMARSS GQLLCTFAGV
QFSQLPIAKL EILLEGANGK TNTENTRLLP IKDRDVQPSR SAPFEFSRLA TPIEASPKPG
EIQSAETVLV ALKEIASTYN SLPAGDIKDD ATMADLGIDS LAAVELSEDI SDRFGITINS
TEILCGTIAR LAQSLLQIEP LVPPKTDAPQ PIEVVDKQEP VVTSALSAIH SNATHGKVLH
LVHEATGIPI EDIRESATLQ DLGADSLSFV ELKHELERCF GVNLDEAGIS AASRVEEILG
ILISPDSSNV SEVYSAYDTP VTSNSSFYAE TKASAFAPHA GLNNAHTLLA QSMERFETKA
QEHNFDQYWD IVNPEQERLL VAYIVETLAQ MGVHLQAMRP GDLLPSLVFN KKHQKVVTRL
LKVLEQHGII DFADDGVGQR YARASGEVPA KTAEELSAEF SRKHPAFSCE ANLMGLTGPN
LAPCLCGSAD PVALLFGSPA AQETVARFYK SSPMMATMTE QLVDYLEMML QQSDHHASIR
ILEVGAGSGG TTARVAQLLS EYAAIKQLKV QYVFTDISAK LVRKATAKFA QYSFISYKVL
DLENLTEEFT QGSPFDIIIG TNCVHATSDR TAVCAKLQTM LCPDGGLLIL SEITDVANWY
DSVFGLLDGW WMDSSNAYAI QPASYWMQSF KKAGFTSWSY STGPTREANS QQLLIAANFA
PALAGPPASP VSRLPATLVD VFSIETAVYK RVDATSIHAD IYFPAKCSSS TPMAI
//
