ID A0A179F3Z5_METCM Unreviewed; 3945 AA.
AC A0A179F3Z5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Hybrid NRPS/PKS enzyme {ECO:0000313|EMBL:OAQ60136.1};
GN ORFNames=VFPPC_10573 {ECO:0000313|EMBL:OAQ60136.1};
OS Pochonia chlamydosporia 170.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ60136.1, ECO:0000313|Proteomes:UP000078397};
RN [1] {ECO:0000313|EMBL:OAQ60136.1, ECO:0000313|Proteomes:UP000078397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:OAQ60136.1};
RX PubMed=27416025;
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT genome mining.";
RL PLoS Pathog. 12:E1005685-E1005685(2016).
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000256|ARBA:ARBA00004685}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family.
CC {ECO:0000256|ARBA:ARBA00029454}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:OAQ60136.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSBJ02000009; OAQ60136.1; -; Genomic_DNA.
DR RefSeq; XP_018138046.1; XM_018288916.1.
DR STRING; 1380566.A0A179F3Z5; -.
DR GeneID; 28852910; -.
DR KEGG; pchm:VFPPC_10573; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000078397; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19532; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; 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; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
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:UP000078397};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2357..2434
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3509..3588
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2443..2512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2443..2462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3945 AA; 430983 MW; 212EF2598B6D901F CRC64;
MAQSNEPIAI IGSSCRFAGG ASSPSKLWDL LLNPRDVASA PPESRFNLDG FYHDNAEQHG
NTNTHGGYFL QEDPRCFDTV FFNISPKEAE AIDPQQRILL ELTYEAMEAA GLTIQGLQGS
DTSVYVGLMI RDYMDVQVRD PDYFSQYMVT GTSSALNANR ISYFFDWHGP SLTVDTACSS
SLVALHQAVQ GLRAGESRVA CVSGTNLLLG PELFISASNM HMLSMRSKMW DVSAEGYARG
DGFVTFMLKT LSNALADGDH IEAVIRETGV NSDGRTKGIT LPSPEAQTAL IKETYQRAGL
DITKSEDRCQ YFEAHGTGTQ AGDPREASAV NDAFFGHDGT TSDDTKNAGK LIVGSVKTIV
GHTEGAAGMA GMMKTLLAMK HGVIPPNLHF HNLNPSVAPH YTHLQIPTTP TPWPRLQAGS
PLRASVNSFG FGGTNAHAIM ESYHPDTENA MLTSNEGSDK CFPAPLLFSA HSEKALVAMV
DDYATYLQQN EDIVSLRDLS WTLRARRSVH SFKVTFSGTT VSDIAQEMKQ KAEAARANPG
TDLGIRSKFV GKKPCILGVF TGQGAQWPTM GKDLILNSKL FSDTIGRLEK TLNDLSDGPE
WSLRQEILAT KSESRVAEAA LSQPLCTAIA IALVDLLHAS GVTFSAVVGH SSGEIGAAYA
AGSLTADEAI KIAYYRGVYA KLAKGKDGIK GAMLAVGMGF EDAKDFCNQP QFASRLTIAA
SNSPSGVTLS GDMDAAKEAK ELFDSQKKFA RMLQVDTAYH SHHMLPCAKP YTNSLLACNI
QAKSPSELPC SWISSVYGSE GTPTAEELAS SYWRDNMAQT VLFSQALERA AIECGPFDAV
LEVGPHPALK GPASQTIREV SDEAIPYVGV LDRKKNDAVA FGDALSFMWL QFGPSAVDFE
GYAAASEPSE PYVAPVLVKD LPLYPWDHSQ VYWRESRLSK EFRCRSAPPH ELLGHIMPGG
NNDNFIRWRN LLRLNEVPWL GDHRFEGQPI VPTSAFCLMA VEAALKWAAA NGLTQTVEVV
ELHEFAIHSA VIVPEESQGA EVISSIQSST SDCDGDRLCC AEFVALSGPP DGSKPLKKAA
SAKVVLFPSG VTADIPTSSR APDDSLTPID GSEFYSSISD MGLAYEGPFQ ALQNIRRRWR
RASALFDKSQ SSHHASLTVD PFFIESCIQV AYAAFSEPGD TSLWSSFLPG SIDKMSINVS
ALSRSDRWLE LDGYITKSSN ATTSSSAAFD ADVEIFDSSS GRLLVEFEGL TVASFRPASA
DDDRELFCHT VWKPDLAGDV VCSSEKRTHD SEKAALALEE QSWRFLNSVR SKWTVCPHAV
SPAFQSLLQF VTHSKNADSF PTSQTSLHAT DSASMRAIIE LIPDLLKGRT PTIDHAIRAF
VERHSVFTRV NSSIRHAIDL ISHRFANLKV LELGSSHLGP SKFVLEGLDD SYSSLTFAST
GLPEAVNAAR VNYVSLEALR LGKPLLNGAI GEEKFDLTIA FYALHGRDST TVEQALEELR
HSIRPGGFLI LVEPTKEFAW SRLFLNALLA SDGGGDSPRD VGSPLSMVQL DRILRKTGFS
GIDSQSPSSS EGPSDAISLI VSQAVNETID LMRRPLQPSA MSLLDDQRLL IVGGRSLPTN
RVIQNMALSL RPWTTSISTI DSFDDLQLDK RQDFAGAIVL TDIDQPLVEL LTMTTYEKIQ
QLFKLVPHIL WVTDGSLNAH PQQAASIGLG KSISEESPSA QLQFLDVESI ENCEEKILQS
FIRLLVSSLP DKANESRLLT VEREIAIRDG REMIPRVLPI KDMNDRLNSQ RRQIKQHLQI
VDTGISFIPT GSMEAATWYA KPTRTHAKPT KVKPITISYS LPFALKVSSG TFLYLFASHG
DGSGAVLGLT ESLSLPGPVC ATWKVPSAVD LGSVTIDRLL EIASGLFIAE NIFQMLPAGE
SLIFEPEPIV ASAISDLCKG SKKTVYFVTT RAEQESGDKS WIIISSQASK RTILSSLPGS
VRLFFDASLR PNRLVSRILQ FLPGDFEVCD QSQLFQLSTR VSKSVTPTTL HLVLQSVGIA
AVKAAKKFPD GQLRKISVSE LLDRLPKCYA GLGIVDWTQT NSIQATIEPL NPDTLFSAQK
SHLLVDVEPQ LQQSISDWLI LHGVRNLFIS SKSRSKPTWR GTPPGTSVQL VEENPANPQQ
LQSFMNSLSD VGGVIYGGAG PRKSFDDKCQ DVLQQWRTTM YELQVLTDVL KVKKPAFFLA
ISSMRKEYAP VNSYLSSLIS QSRSHGIPAS LVNVDAIWSH TDSLTTSPFM RISECDLHYV
LGEAISSAKA NSHHPEVLAG IKRFEPGNAS ENIKNRWLSY PLYSHHYLRH RGVNQDDAQL
QAQNLKQRLA TCQNLDAASK TIQQFFSSRL AVMLNLPPES IRPDNDLTSL GADSLSASDI
RSWFLRELDA DVPVLQILGG ASIAELCDEV ASKLALEIGQ ETPNVEESIT SPPIPSRQTD
SINTAPEEKH TTENPGNQYI SASSSDGYTT TTDTGEAAPT PQTEAVPDSG YVSPHKLDLP
AVKYTEKMSY SQNRLWFPSV YLDQKTPFNC TTSYRLTGPI DASRLNKAFH LLIQRHESFR
TAFYNDPCTG EPTQSILTSR PFVLKVSSGN GTEDVDREFR QIAEYHFDLS IADTLIATLV
SQGPDEHTII FGYHHIIMDG VSWQITLNDL AQFYDSETAN LPSLAQYAEF TAKQRHLVSI
NAHADKLAYW KKEIPVTPSP LPLFPFAKVS TRKALTRYNT LDYIFDVSPT LVAKIKKASL
EAKCTSFHFY LSAFVVLLNR FLDLNDVVLG IIDANRHDKS FLNTVGFLLD MVPLRLKVNK
KERFLQTLRN TRGKAYGALG NAGVPLETIL KELQIPTSST NTPLFQVLIN YRMGALRAPQ
MGDAKMSFLN YEDAKAPFDL AISIDEKDDG SGMLTFSMQD YMYDQEGAEL LVTTYVDLLD
SLATDTSQRL NEVSMSKTLS SKALIAGTGP VIDFQWPNTQ TLSQRVDWQT EQHPDALAVK
DMAGASRTYL ETQKRVFAIA LALGEVGITH GSRVAVYCEP TVDSIACILA IHRVGAVYIP
LDVRNSNERL EAVVTECDPG LIIYHLATKD KLFAFSGLTP TVDLSTIPET ADSIMPNVSK
LSDPAFILYT SGSTGKPKGI MLTHANCSIH FASISNSLGL TNKHVVLQQS ALGFDASLSQ
MFMALSNGAA LILGSNRGDP ADLADLIRRE RVTVTLFIVS EMSALLQHGS HILSECRSWR
IALCGGEAFT VSLLQKFRNL GLQDLTLYNA YGPTEATIIT SLGKVEYHDD NWGDDPKVPV
GPPIPNYGVY VLDDKLQPAP LGWPGELCVC GPCITTGYVG QPDLTAAKFW PDQIKKPVGT
VYDGWNTIYR TGDKARQLSD GSFAFLGRID GDSQVKIRGI RIELGEISNA IIQSSKGAIS
DAATIVKGDT HQTLFSFVVF SADYRSKAGQ QEASTTYLRK LIQSLPLPVY MRPAIAVPLD
RLPFTERGKL DTKSLSAVPL EVDSEDAPEN LTLTEQKLRQ VWQDTLADQA LPIPIRKQSD
FFSVGGNSLL LIRLRKSIKD AFDTSVPLAD LFQASTLEML AAQLDRTNSP KLEQVDWEAE
SALDATLPTI NVSQNADREG TPITILLTGS TGLLGREILR QLIASDRILK VHCLAVRPGR
KLPDDLASSK KIVLHSGDLA APRLGLEESV AQDLFSSSAA IIHNGAEVSH MKSYPSLRIT
NVGSTRQLLD LAVRVSRACD TPVPSFHYVS TAGVGGLPQT ASFEEISVAP FPPATDGSNG
YVAAKWASER ILERAAEKLG LPVAIHRPSN ITGTDVGDRD IVHSVWRWSE SLRVVPDLAS
AGAQGAFDFV GVDTCARGII SSVFRRLERT DNATVEYIHQ SGDTVFPIDS FKDVLDGRLG
TEVSLLPFRK WVDKAEKAGL DELVAAFLRQ TNGAFRMPLL VKRET
//
