ID A0A2H3I7B4_9EURO Unreviewed; 2259 AA.
AC A0A2H3I7B4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acyl transferase/acyl hydrolase/lysophospholipase {ECO:0000313|EMBL:PCG90706.1};
GN ORFNames=PENO1_097720 {ECO:0000313|EMBL:PCG90706.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG90706.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG90706.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG90706.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCG90706.1}.
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DR EMBL; NPFK01000469; PCG90706.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3I7B4; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase 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:0006633; P:fatty acid biosynthetic process; 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; 3.40.47.10; -; 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 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-like_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; 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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 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; 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 Hydrolase {ECO:0000313|EMBL:PCG90706.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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:UP000218381};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PCG90706.1}.
FT DOMAIN 29..454
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2176..2253
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1289..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2259 AA; 247104 MW; 4F0E05499EBC8B88 CRC64;
MNGFSDIPDT HPASPTLNHD VSCCDEHNRQ RIAIIGYACR LPGDVSSPAD LWELCTRKRS
GWSPIPKDRF ASGAFHHPNP SKVGAFNPSG GYFLQDDISR FDAPFFNITA QEAISMDPQQ
RLLLECSYEA VESAGIPKES LAGRNVGVFV GGNFADYELH NVRDVETIPM YQATGCAPSL
QSNRISYYFD FRGPSFTVDT ACSSSLVALH AAVQSLRSGE STEALVAGCR LNIVPDLFVS
MSMSQLFNDE GRTYAFDNRA TSGFARGEGA GVVLLKSLDD AIRDKDPIRA VIVNSGVSQD
GRTQGITLPN GHAQEELIRR VYNEAHIDPE DCGFVEMHGT GTKVGDPIEA TAVHAALGHG
RSPRNPLYIG SVKSNVGHLE GASGVISLIK AAMMLDRDLL LPNADFKKAN ENIPLTEWNM
KVVTSTRPWP RGKRFISVSN YGFGGTNAHV VLEKAPLSLN SPDSFSTDTD DTTDNDPKHK
LIFISANDKQ SLVQRIKDFG IYFEQRPEVF EKLLFGNFAF TVGSKLSHLS YRIALPACSL
DNLGIRLAQL KVNAPKVLGD PKIGYVFTGQ GAQWAQMGCA LMEYPIFKAV IQQADDYLRQ
LRAEWSLEEE IKKDLAESRI DSPELSQPAC TAIQIALVTL LESWGIRPNY VVGHSSGEIA
ASFAARIYDL HSAMALSYYR GQMTRLLKET HPSLRGGMIA VGAGASTVRP MLKMLRTGYA
TVACVNSPTS VTVSGDVSAI EEFEHVLQTE QIFNRRLRID VAYHSDHMKR ISDAYFTSIA
HIHPKSTLQN DVVFFSSVLG CVAETSTLNA SYWVQNLTSP VLFPDALEQM CKQDGEIPNL
LIEVGPHAAL KGPISDTLKH LGLTSAKIAY APTMVRKGNE VETLMNTAAA AYVRGANLDP
YAINFPRTGA QNHSFLTDLP RYPWQHHTRY WHEARIAKKH QMRDGERNDL LGVMANYSND
MEPTWRNILR LDDMPWLRDH KMQGMVVYPL AGYLAMAIEA AARRAHQRNI TFAAFEFREV
VVESALVLTD DVDVEITISL RPYEEGTRGA SDVWDEFKIH SWSSQRGWIN HCHGLVGVRN
SLDGGASGTF GSGLKSRSHI QSRKSKILSS SANHVPDDRL YQVLTDLGAD YGPTFKGLEN
CYADSHHSHA DLHIRDTTAL MPKNFQSPLH VHPAFLDGLL HLVWPILGHG RMALDTLYMP
TLIKHAIISS DIPFAAGQHV RAFGTGSPNL PSPEPTHFDL FAVAEDSTAD PLIMLDGLVM
TPIRDGGIEV GSVIRKLCYK LEWQPWENQS NASNGHAQPT KMSNGQAHEL TNGHSQFGVQ
NDQNGINGSK HNSSNGLNGH HQVNGSCSTH DDIQDLPTEQ TINNRVVILR FSRERENDPI
ATEIAKDLGQ SPSESLLVTE SETQCTDSHV IILQSPDASL RDATATEFEA IRRILLTAAN
ILWVYANNSP DAQMTVGMTR SVRSETMAKI VTLGIHSEDP IIAASTVSTV MDAIWPTDGV
APCKESEFKS TDSSLLVLRA VEDISSNAFV HNENSDISLS KQPFHQPGRR FKLKIAQPGS
LDTIYFTDDD VAELADDSVE IEVQATGINF KDVVVSMGQL NQPYIGVECS GIVTSVGKKV
TDIIQGQRVM AMPEGAYSTY ARCPSTSTAP IPDSMSIEEA ATIPIIFCTA YYGLFDLGHL
SAGERVLIHA GAGGVGQAAI QLAQMAGADI FVTVGSHEKR SFLMEHYNVP EDRILYSRDN
SFGPAVRRAT DNEGVDVVLN SLAGDLLRES WDCLAPFGRF IEIGKADITK NSRLEMSKFE
HNVTFASIDL TKVAKFRPKL MKRLLSDVCR LLSDGAIKPI YPITKYSISE VEAGFRALQT
GKNMGKSVVV PNTDDQVKAV SLKTSSSILR KDATYIIIGG TGGLGRSMAK WMSTKGARNI
VLVSRSGSIN EKLEALIHEL AHHGTQVLVK VCDVSSRANV ERLVNVELTH LPPVRGVVHG
AMVLRDMLFE NMTLDDFQSV IACKVEGAWN LHHCLAQSPL DFFIALSSVS GVVGNRGQAA
YSAANVFLDG FMEYRQSQGL PGKSINLAAV TEVGYLAESD PSRQQEVEKN IGGATINESE
VLALLALAIT SDLNKSNQSQ FVTGLEATDS LDSFWLHDSK FSSIREAVES AMNELQKGGK
ELPLRVAVQS APTRANAIHI CYEALATKLA AVLGMAPEDM DVSTRVSSLG LDSLVAIEIR
NWIAREADAN VQVLELLSSE SLIKLAELIL AKSKLSIPE
//
