ID B6H9P1_PENRW Unreviewed; 2538 AA.
AC B6H9P1;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Pc16g11480 protein {ECO:0000313|EMBL:CAP93818.1};
GN ORFNames=Pc16g11480 {ECO:0000313|EMBL:CAP93818.1}, PCH_Pc16g11480
GN {ECO:0000313|EMBL:CAP93818.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93818.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP93818.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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DR EMBL; AM920431; CAP93818.1; -; Genomic_DNA.
DR RefSeq; XP_002561451.1; XM_002561405.1.
DR SMR; B6H9P1; -.
DR STRING; 500485.B6H9P1; -.
DR GeneID; 8307613; -.
DR KEGG; pcs:Pc16g11480; -.
DR VEuPathDB; FungiDB:PCH_Pc16g11480; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; EYGIDSH; -.
DR OrthoDB; 5396558at2759; -.
DR BioCyc; PCHR:PC16G11480-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c16.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR011032; GroES-like_sf.
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; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; 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; PF08242; Methyltransf_12; 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; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..458
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2538 AA; 278677 MW; 7D02931A5665B6E8 CRC64;
MSPQSSVRPP KATISEDDLA NSAAGSCIPI AIVGIGFRGP GDAKNVEGLW EMILTGKEAW
SPIPATRWNS AAFHHPDHAR HGTINVEGGH FLEEDVSVFD APFFNMTSDE AAAMDPQQRL
LLEVAYEGLE NAGIPLANTM GTKTSCFVGS FSADYTDLLL RDPECVPMYQ CTNAGQSRAM
TANRLSYFFD LKGPSVTVDT ACSGSLVALH LACQSLQTGD ASTAIAAGVN LVLSHEFMST
MSMMKFLSSD GRCHTFDEKA NGYARGEAAG CLILKPLAKA LHDHDKIRAV IRGTGSNQDG
RTAGITLPNG AAQESLIRSV YARADLDPSE TDFVEAHGTG TLAGDPVETG AIARVFGIGR
PPDNPVRIGS IKTNVGHLEG ASGVAGVIKA VLMLENRMFL PNRNFEKINP RIPLDDWKLK
VRIFGQVESW RLTSVGPRRV SVNSFGYGGS NAHVIVEDAQ GCLSNWGLDE HHTIISTTTN
NHAETLLSSP LALSRIFMVS GFDERTCAQQ MQALSNYISD RGHEVDQEKF LDDLAFTINE
RRSVFPWKAA VVGDTIAGLA TSLSQNVKAR SAVRNPRLGF VFTGQGAQWA GMGKELLQAY
PIFKVSILAI DKFLIDMGAP FTVEGEIAKH PRDSDLNHPS LSQTVCTALQ IALVDLLKSW
NIYPDSVTGH SSGEIAAAYA AGALSMYDAM SVAYYRGVVA SQLLHDQPNR GAMMAVGMSA
EEVQPYLDEF QPRQLVVACI NSPSSVTISG DILAIDALGQ TLKDQQVFSR RLEVGVAYHS
PHIEQVAEQY HSLIGHIQPR GLDQITEDKR GKWPLFFSSV TGKMAPLQEL HARYWVSNLV
GQVKFAQSLR TLCFETNSQR GGNTGATRIR RAGAAQKPSV DCLIEIGPHA ALSGPINQIL
QADAKLNAAD IAYISILTRK TNAVTTALGA VATLVSLDYP INFGTINRPA GAKKDSTPQL
LTNLPTYVWN HTRSYWAEPR LSKMYRNRIS SRMDLLGTPD NMACPFEPRW RNYIRTSELP
WLLDHKIQGN IVFPAAGYLV MAIEASIQLN KEEKIARYIL RDVAIQSALV LSETSAVEVM
VSLQKSTQDQ ERLYNFHIYS ISEENRWIEH CTGLVGTQKS IGASGDGAED TDGYATVPLG
TEVHGVSVID VRDFYEKLQI SGLEYGPCFA NMTKARATKD GACFAEVTVP DTLSVMPASF
QHELLIHPCT LDSIFQTIFA ALPRGMGIEE GPAIPVSIEE MVVSSRLSCS AGEPMSICTN
VRPMPNKDVM AYIVAVNCNE KQFETEPTIS LRGLRCARLG RHEPVSQTKD SIIYQINWKP
DPSFLSSDNA SFIFTETSTV QEPARQKEYE EIAASFIRAA LEEVSKTEAM KLDTSHRRFR
CYLQDVLERH DDNRSISPAH SENIHSIPMG RLLPVIGQNL VAIIRNQVDF STVIEDDRLL
DEFWDIFSAD TSYRAAAKYV NLIGHRKPDI SILEFGVGTG QVAEIFLKHL VTLNETPYCG
KYTFAHESAS VLEHTSKRLE AWSEWVECKP LDLDKDITEQ EFERNSFDII ILPHGLCTAR
CEENALSKIH DLLRPSGYLI AINPFHPKKN VLKNLLFSAL HSLSADEFCL GQSGWTESQW
DEILQDAHFT EVDAYADQDT EKSHQFIVAK KGKIHQSSRK VSIICGDKAE ARYLDTELEK
ISCEVNVTHV NNLECKEQIC LVLDTSKSSL LASANEVTFS KIKSLFTQSG GVLWITRGGT
IESVNPTAAL AVGFARTARA ESGVNPIITL DLDAQNPLSE SQAADIITKV LVTRFLHESS
DEDTEYAERN GQILVPRVLE NPKANKTMNS INDTDAISEQ PFHNLQQPLR LSRKFDNPGF
VGDLQVTDLP AGYVGIKVLS FGLNKWDVQP DYFDWETDDT LGMECSGIVY KVGAGIHDIT
VGDRVACFGT GTAKSFYHDR ASAFQKINGE MSLQMASTLP LAYTVAYYVV NHLSMVESND
AVLVHDAGSH FGQALLEVYL LTDARIFATV YSPDEKDLLS SRFGIAREHI FISGKDDVAK
GVSRLTEGKK ANVVVAFETA EERILQNSIA PFGRLIQLQT SNLKARLLSC PPNISLSTVN
MRERRDLVNQ IWPKVFRLFL EKRLKGPGFT GVYHVSKIQE AIAAIQTKQH VVVQVEDSDV
VTATLPRATQ PLFQANASYM LVGGLGGIGR EVALWMAENG AKSLIFVNRS GLSKYESQMT
VRNLVEKGAQ ITTRACDISD ETAVQRMLQD LSYSVPPIRG LIQAAMVLKD VHIENMRLDE
YRDVMGPKYH GTWNLHRHLP ADLDFFLMLS SISGVIGNAT QAAYASGCTF MDAFAAYRRS
LGLPAVSLDL GTITDVGYLA ENRDLATKME RQGFQGTDTP TLLSLIQVAI SQSTGGAAQL
VTGLGQWKEM ESLGNFDAPL FAHFRYKFQG HGKSIALGDS MEGLKVDLDA AKTVDQATII
ICDALSRKIA SHLSIPVENI NPSNPVSEYG VDSHVAVELR NWVSRSMNCT IPILEILARS
MFELSHKIAS QRLEGNSE
//
