ALT5_ALTSO
ID ALT5_ALTSO Reviewed; 2551 AA.
AC Q5KTM9;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Highly reducing polyketide synthase alt5 {ECO:0000303|PubMed:16356847};
DE EC=2.3.1.- {ECO:0000269|PubMed:16356847};
DE AltName: Full=Alternapyrone biosynthesis cluster protein 5 {ECO:0000303|PubMed:16356847};
GN Name=alt5 {ECO:0000303|PubMed:16356847};
GN Synonyms=pksN {ECO:0000303|PubMed:16356847};
OS Alternaria solani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Porri.
OX NCBI_TaxID=48100;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RC STRAIN=584;
RX PubMed=16356847; DOI=10.1016/j.chembiol.2005.09.015;
RA Fujii I., Yoshida N., Shimomaki S., Oikawa H., Ebizuka Y.;
RT "An iterative type I polyketide synthase PKSN catalyzes synthesis of the
RT decaketide alternapyrone with regio-specific octa-methylation.";
RL Chem. Biol. 12:1301-1309(2005).
CC -!- FUNCTION: Highly reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of alternapyrone derivatives
CC (PubMed:16356847). Alternapyrone is a decaketide with octa-methylation
CC from methionine on every C2 unit except the third unit
CC (PubMed:16356847). All the domains in the polyketide synthase alt5 are
CC apparently involved in alternapyrone synthesis, that is, the 8 CMeT, 7
CC KR, 7 DH, and 4 ER reactions in the 9 KS-mediated condensation steps
CC required for alternapyrone synthesis (PubMed:16356847). the
CC alternapyrone produced by alt5 might be intensively modified by
CC cytochrome P450 monooxygenases alt1, alt2 and alt3 and FAD-dependent
CC oxidoreductase alt4 present in the alt gene cluster (PubMed:16356847).
CC {ECO:0000269|PubMed:16356847}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250|UniProtKB:Q9Y8A5};
CC Note=Binds 1 phosphopantetheine covalently.
CC {ECO:0000250|UniProtKB:Q9Y8A5};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:16356847}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC (CMeT) domain responsible for the incorporation of methyl groups; an
CC enoylreductase (ER) domain that reduces enoyl groups to alkyl group; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:16356847}.
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DR EMBL; AB120221; BAD83684.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5KTM9; -.
DR SMR; Q5KTM9; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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; PF08242; Methyltransf_12; 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; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..2551
FT /note="Highly reducing polyketide synthase alt5"
FT /id="PRO_0000444928"
FT DOMAIN 2467..2544
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 5..429
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16356847"
FT REGION 450..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..905
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16356847"
FT REGION 961..1275
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16356847"
FT REGION 1444..1622
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16356847"
FT REGION 1853..2166
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16356847"
FT REGION 2189..2366
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16356847"
FT ACT_SITE 175
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 672
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 990
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2504
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2551 AA; 277636 MW; 65505CC8F5BB95D0 CRC64;
MDKPVAIIGI AFRGPGDARD PEAFYRMLVE GRNARTEIPK DRYNVDAFYH PDSERLGSIQ
QRHAHFLQQD FKVFDAPFFS ITPKEAKAMD PTHRILLEAT YEGFENAGLS LEKVSGTQTS
CYIGTFTADF PNLQARDNEG PSIYHATGMS ASLASNRLSW FYNLRGPSLT VDTACSSSLT
AFHLACQSIR TGEAEMSVVG GANLMFGPDM SILLGAAKIL SPEGKSKMWD ANANGFARGE
GFGVTILKPL DAALRDGDNI RAVVLATAAN EDGHTPGISL PNSEAQQELI RRAYQIAGVD
PAETAYVEAH GTGTQAGDPL EARAILKTIG SVEGRKSDLY VGSVKTNIGH LEGAAGVAGI
IKAALTVERG MIPPNLWFEK LNPEIDLPDN VKIASKLTPW PHSGPRRASI NSFGFGGANA
HAILEDAASF LSRHGLSGRH TTAPLLPSLS SVRVSHPSDS PSSSASTVAE EATSGESSDN
ISDVSSEVLR DVYPIPKLFV LSSHDQEGVK RSAERLQEYL ASKTSTTPSF LNDLAYTLSA
KRTTLPWKSY AVSSSVSGLR EKISSLPPVV RSSTSAIPRI AFVFTGQGAQ WHAMGRGLSV
YKTFAESLQR SEVMLKSFGC PWSLAEELSR SKAEYKLRET DYSQPACTAI QVALVDLLSG
FDVRPVAVLG HSSGEIAAAY AAGFIDQEAA IKIAWLRGQV NKTVSKNGGM LAVSASADSI
QSHLDGLKSG KAVVGCFNST KACTVTGDTS AIDELQTMLK DAQVACTRLP MDVAYHSFHM
EAAREKYEQA LEGIAHGSTS TIPMFSSVTG TLVDPAQMKP SYWVDNLVSP VNFVAATRSL
LSHPQESKSR KAFANLFVEL GPHSALRSYL LDIISSENRA ADTTYTTLLR RNFDGAATAL
EAMGHLWAHG CKVDLSKVND VSSDSTNMLI DLPPYAWNHK PYWDESHLSR QHRLRKSPRT
DLVGYRLLGT PEHTWRNFLR CNENPWIREH KVQGDILYPG AGMLVMAIEA AHQLAQETSA
DEIYGFELRD VSIDTALRVP DTEKGIEVMT QLHNRRTGTR AAPSSTLYEF TVSSWSEEMS
SWSTHARGLV SITFKTFSPS MEREVALGNE RYMSSLAEVR RVCQTPARSF LYDTVETIGM
QYGPTFRNMT ELYAGPNSSY GVINVPDTKA IMPKGFEFPH VVHPATLDSV LHLIFPSISG
EDQALNEAVV PRSFDRIFVS ASIPKNAGAE LRGCSSAKKL SYTTWNSNIT MSDATMTEPV
VIMEGVVLAS VGATEDASKQ LETRASCFAQ NWHVDADLLT PSQIKEIIYK RTLKSKDDDS
VLDLLEFVCL VYIYRILDWF QTEEGKPHVP RDGFWKSYVE WMHDTVKQFP ALPADVETEM
EKARQRIVKS ESGDITVQMV DRIGQNLSRI FTREVEALQC MTEGDLLYSF YRGAFGTSFN
TNVAEYVGLI ADKQPGLRIL EIGAGTGGTT YHVLERLRNP DGTSKAAQYY FTDISPGFLA
KAADRFNQDA SIMQFGTLNI ENAPTEQGFS PELFDLIVCA NVLHATKSIQ ETLTHCKLLL
KPGGRLVLSE VTIKRIFSGF IMGPLPGWWL GEADGRMGGP LLDADEWNVA LKKAGFSGVD
VDVRGDRETS KEPVSLLIST KPKTTAPSLP SCLVITTGTE ASNMLADTIQ RVFTSAGHDI
SIAQWNSVTK TQVEGKYCLC LAEWEDAILV NLTDDDWDRL REVVLSSEGA LWITGGGALD
TPFPMKSLMV GLGRAIRNED AGVRLACLDL DPPTTIDFEE ASRTTLKVAY AHIRGDGTEG
EFAAHGDKVY VPRVERTLQV DGSLRKYEAK GDPEMVPFKS CGRPLKLTIK TPGLLDTFQW
EEDETYHTPL PEDWIEIEVK AVGLNFKDVL VALGNLAENK LGVDASGIVT RVGSAVTNVQ
VGDRVMTASC DTFATYVRFP AKGAIGVPTG MSFEEAASMP LIFLTAYYAL VTAGGIVAGE
KVLIHAAAGG VGQAAIMIAQ AKGAEIFATV GADTKKQLLI EQYGIPEDHI FSSRDTSFVK
GVLRATDGQG VDLVLNSLAG EALRLSWTDC LAKFGRFLEI GKADLFANTG LDMKPLLDNK
SYIGVNLLDF ENNPTPRAVA LWHDTAKMIH DGAIKPIAPL QVFTMAEVEK AFRHMQAGKH
MGKVVVRVDD ADVVRAVPRI PRVSIHPDAT YMIAGLGGIT REIARWLAEK GARYLVFLSR
SAASGTDNQA FALQLRNTYD VTPLAYDCDV GNKAALQAVL DDLKAKGLPP INGCATGAMV
LQDCLFDKMT ADHVRTTVGP KVHGTWNLHE LLPRDMDFFV MLSSLAGVMG HRGQGNYGCG
NNFQDEFASF RRGQGLPAMT IDIGYLLSVG FVAEHDEYVD HVKAMGLKVM HTSDLHGLVA
TAIEGPSQHP GQVMCGLPFN EHDDAWYWMA DARFAALRNV AAGSAANAGQ AISLREELTR
CGTVNEEAVQ LITAAIAQRL ASLMMIPEAD IDAGRPLSAY GVDSLVAVEV RNWVAREMAV
EVSVFDVMQN VPMTQLAQNL AEKSKLLLGQ A
