ID K2SDY5_MACPH Unreviewed; 2086 AA.
AC K2SDY5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN ORFNames=MPH_02141 {ECO:0000313|EMBL:EKG20614.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG20614.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG20614.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG20614.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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 -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000256|ARBA:ARBA00004685}.
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:EKG20614.1}.
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DR EMBL; AHHD01000083; EKG20614.1; -; Genomic_DNA.
DR STRING; 1126212.K2SDY5; -.
DR VEuPathDB; FungiDB:MPH_02141; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; K2SDY5; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
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:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
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: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; 3.30.70.3330; -; 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; 2.
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; IPR041099; FAS1_N.
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; PF17828; FAS_N; 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; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
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:UP000007129};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1690..1990
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 282
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1834
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2086 AA; 232141 MW; BAAD1513271A7050 CRC64;
MYGSGPQTGV STPRSQAHLR PLILSHGSLE HTFLIPTALH FNASQLKDTF LSTLPEPTED
RAQDDEPSSE CELVARYLGF IAREVEEGDD PGSFEEVLKL VLNEFERAFL QGNEVHAIAA
HLPGIEAKKL TVVSAYYGAR AAVDRPIKHH DSALFREAAD GNAHIYPVFG GQGNIEEYFE
ELREVYTTYP AFVEDFVNAA AAHLQTLSRD ERVAKQYAKG LDVLRWLNNK ESQPDTDYLV
SAPVSLPLIG LTQLAHYVVT CRVLGSHPGH LRSYFSGTTG HSQGVVTAAA ISASKSWETF
DKASRDALTI LFWIGSRSQQ AYPRTSLAPN VLQDSIDNGE GTPTPMLSIR DLPRKAVEEH
IASTNEHLPK DQHIAISLVN SARNFVVTGP PISLYGLNLR LRKVKAPTGL DQNRIPFTER
KIRFVNRFLP ITAPFHSPYL AEATKFLDED LKDIVIPSEN LGIPMFHTAT GKDIREDKEA
NIVPALVRMI TQDPVNWEQA TVFPNATHIL DFGPGGISGL GVLTNRNKEG TGVRVILAGT
MDSTNSEVGY KPELFDRDSE HAVKYAVDWV KEHGPKLVKT SAGQTFVDTK MSRLIGLPPV
MVAGMTPCTV PWKFVADTMN AGFHIELGGG GYFMDSMMTD AIKKIEQAIP PGRGININVL
YVNPRALSWQ IPMVARLRSE GVPIEGLTIG AGVPSIEVAT EYIETLGLKH ISFKPGSMDA
IQQVINIAKA HPTFPVMLQW TGGRGGGHHS FEDFHQPILQ MYGRIRKCDN IILVAGSGFG
SAEDTYPYLT GVWSTKFGFP PMPFDGCLFG SRIMVAKEAF TSPAAKQAIV DAPGVDDSEW
EKTYKGPTGG VITVRSEMGE PIHKLATRGV LFWAEMDQKI FSLDKAKRLV ELKKMRDYII
KKLNDDFQKP WFGKNSAGEA VDLEDMTYGE VVRRMIELMY VKHQSRWIDV TLRNFTGDFI
RRVEERFTTS SGKPSLVQNF TELEKPFEFV EKLFKEYPEA DKQLINAQDV QHFLMLTMRV
IQKPVPFVPA LDENFEFYFK KDSLWQSEDL DAVVDQDVGR VCILQGPMAA RFSTKVDEPV
KEILGGIHEG HIKHLTQDLY GGDESKIPVV EYFGSKLLGA HDDVAEVEGL TVSEVPDKTI
YRLSSAPNAT LPDITSWMQL LAGKTYSWRH AFFTADVFVQ GQRFQSNPMQ RIFAPTLGMM
VEIAHPNDPA KTVITMREPS HGGKHIKTVE ISLQGKNEVL VNMIEERSAL RKPTALPLKF
TYHPDCGYAP IREVMEDRND RIKEFYYKLW FGDEQCPFDA SVTSTFEGGR ATITGEAIND
FVHAVGNTGE AFVDRPGKEV FAPMDFAIVV GWKAITKPIF PRAIDGDLLK LVHLSNEFRM
VPGAQPLKKG DVLDTTAQVN AVINQDSGKM VEVCGTITRD GKPVMEVTSQ FLYRGAYTDY
ENAFQRKSET PFNLHLATTK DVAVLRSKEW FKLEDGDIDL LNKTLTFKLQ TLTRYKNKSV
FSSVETVGEV LLELPTKEIV QIASVEYEAG TSHGNPVVDY LERNGTKVDQ PVLFENPIPL
HGKSPLTLKA PASNETYARV SGDYNPIHVS RVFSKFANLP GTITHGMYSS AAVRSLVETW
AAENNIGRIR SFHADLVGMV LPDDEIDVKL QHVGMVSGRK IIKIEASNKE TEEKVLLGEA
EVEQPTSAYV FTGQGSQEQG MGMDLYNSSP VAKEVWDRAD KHFLDNYGFA ITHIVKNNPK
ELTVHFGGPR GKAIRQNYMS MTFETVAADG TVKSERIFKE IDEETTSYTY RSPSGLLSAT
QFTQPALTLM EKAAFEDMRA KGLVQSDSSF AGHSLGEYAA LAALAEVMPI ESLVSVVFYR
GLTMQVAVER DEAGRSNYSM CAVNPSRISK TFNEQALQYV VENIAEQTGW LLEIVNYNIA
NMQYVAAGDL RALDCLTNVT NYLKAQKIDI QQLMQTMSLE DVKAHLVEII KECAKQTEAK
PKPLDLQRGF ATIPLKGIDV PFHSTFLRSG VKPFRSFLLK KIHKTSIDPS KLIGKYIPNV
TARPFEITKE YFEDVYRLTN SPKIGNILAN WDKYEEKPQE AAAATA
//
