ID A0A2H3IIM8_9EURO Unreviewed; 2040 AA.
AC A0A2H3IIM8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acyl transferase/acyl hydrolase/lysophospholipase {ECO:0000313|EMBL:PCH03972.1};
GN ORFNames=PENO1_029740 {ECO:0000313|EMBL:PCH03972.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH03972.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH03972.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH03972.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001214};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000256|ARBA:ARBA00001055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000175};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00000343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC Evidence={ECO:0000256|ARBA:ARBA00001540};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00000936};
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000256|ARBA:ARBA00033756}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000256|ARBA:ARBA00010009, ECO:0000256|PIRNR:PIRNR005562}.
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:PCH03972.1}.
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DR EMBL; NPFK01000060; PCH03972.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3IIM8; -.
DR OrthoDB; 2158695at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:InterPro.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd03447; FAS_MaoC; 1.
DR Gene3D; 1.20.1050.120; -; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.2430; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR005562};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR005562};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005562};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1657..1956
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 306..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 268
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1798
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2040 AA; 225683 MW; B5F6D3251C5955DB CRC64;
MDTPLSEKFS GVSDGEFSLR LEKVQSTIFV SREDLEQLKD QRDLFLLGEA STSRPHITSE
IELALSFLQH LLENSGASSS TRSFLQGFEN KYLFEFELHS LLQTSQIDPP TRNKLLSTYY
KAVSLITSEP TSNASSALFS VAKSGHINPY VVFGGQGTAN ATCVKELVDL YLTYTPFLKD
LIDVTGALLS RLSRLPQTRE YYCGRYLDLQ GWLRDPDQVL GSDFISGVTV SCPIIGLLSL
AHYCVTCKVL GMTPGDLRSL LQGATGHSQG IVVAVAIAIS DSWDSFYGAA LTAVETLFWI
GFESNQGSPR SSVSPSVIED SLSNGSGQPS CMLSVVGLER SRLDRILGII NKSLPSTSQV
GVALINTRDN FVIGGPAKSL AALDTYLRTI KADPEIDQNR IPHSKRKPTI QHQFLPITVP
FHTEYLSTPA QKIKDHLSSY IFPEMLEIPV HDNRNGHDIR ELPHGTNVLD NLIDAICTDR
CDWPAALQSS NASHILTFGS GGVPDLVMRL VDGKGVRVIS GSDFETRDPD IGSKLDIFSP
IFLPTSTKVE SWGEKFQPRL VQPSSGSVRL ETRLSRLLGV PPVFVAGMTP TTVPWDFVST
VMNAGYHVEL ASGGYYNAEE MSAAIERVKN SVPAGRGITC NLIYSSPQAM TWQIAMLRRL
AKDGVAVDGL TIGAGVPSQE IVTDYVTSLG LKHISLKPGS ISAIREVIEI AKTQSQFPII
LQWTGGRGGG HHSYEDFHAP ILRTYSSIRK CSNIILVAGS GFGSYEDSYP YLSGTWATRF
GYPRMPFDGI LLGSRMMVAR EAHTSLAAKK LIIEAPGVPE TEWEKTYEGA EGGVITVISE
MGQPIHKIAT RGVLFWHELD KTVFSLPRKN RLETLLKKKS YIIKRLNADF AKPWFGQKAK
GEPAEISEMT YMEILRRLVS LMYVAHQSRW IAPSYLEFVM DIAARTLERL SAKSNIEITA
ASLQSPQHFL EAFARCCPLA STELLNPEDV KYFILRCKKR GQKPVNFIPT IDEDFETFFK
KDSLWQSEDI DAVPDQDAGR CCILHGPVAA QYCNTDKETA KEILDNINKG LIRKVGEGFY
PGGLITQSEN ASLSSESWSV ATPESDSRDI SLTPVDSLAG GVEDLLLSTV LLLGKMGNPW
IRSLFTDECV LRGRERKINP FHRLIQRASK GTVEVDPETS LITIFIENEE SSKNKSTVRI
SSQNDVDISV ELSFPSFHGK EAIVLPLSFR YDQTMTPYGI SEVTASRDDR IKTFYSKVWF
GQDVSSSTED VRSTILGPEM TLTAEMLEDL SNTVGRTHAQ GKNIVSGSDI FPISVGIVAA
WDAVAKPIVL KAIPGDLLRL VHQSNSFEYV TDTALRVGDV IRSKANVRAI YIEDAGKYVT
VEGHILSSSE PVLKVTSTFL FKGYFDDFLS TFKVTDEPDI IFEVISEQDQ AVLKDREWFH
LQDPFLSLIG KTLLFDLRSE VTWKNKTTYN TLKVSGQIFQ RNSLGQIQEI GSVSFEHGEC
VGNPVMDFLQ RKGTPAAAKS DLTSPGWTGV SSVEVQMPNS NEMYTRVSRD YNPIHMASIF
SHWAELPGTI SQGMFTSAIA VNAVEHLSLN GERHRLRKFT ATFTDMVLPG DRLVVRLKHV
GAVDGRLVFK VSGVKADTET VVLEAEAEVD QPQSVFFFTG QGSQLPGMGM ELYKTSEVAR
RIWDEIDAHI FERFVIDIVS NNPKSMTIHF GGKRGRQLRE NYLAMETEIT TPDGRTIRKT
LLPGLTCESL SYTFSCPSGL LFFSSFAQPA IVLVEKIMFE DMKSRGLVPS NPFFAGHSLG
EYGALLAFSG FMTTKELMEL AFYRGLSLQF AMERDSNGET NYGMVAANPQ RIGKFFGESP
LRQIVRMIAT QSNELIEIVN LNVENEQYVC AGTLQNLHVL ENVLSYLATA PHGAELVGEI
MTTKDDLSAT TIGQRLAVNL IEAHRLPSPI RLKRGKGTIP IPGIDVPFHS SFLRQSVASY
RKILQRRIPE ENIHLDRIVG KWIPNVMARP FSIDDDYLQE ALELTQSPLL GKLVNGPVVV
//
