ID M2SVE3_COCSN Unreviewed; 2086 AA.
AC M2SVE3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN ORFNames=COCSADRAFT_235908 {ECO:0000313|EMBL:EMD60787.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD60787.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD60787.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB445649; EMD60787.1; -; Genomic_DNA.
DR RefSeq; XP_007703182.1; XM_007704992.1.
DR STRING; 665912.M2SVE3; -.
DR GeneID; 19134874; -.
DR KEGG; bsc:COCSADRAFT_235908; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OMA; HFMDNYG; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000016934; 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:UP000016934};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1688..2009
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 1832
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2086 AA; 232664 MW; 1899971ACE40F16B CRC64;
MYGSGQQTGI STPRSAANLR PLILSHGSLE YTLLIPTALH FNAQQLRDTF TSTLPEPTDE
LAQDDEPSSV PELVARYLGF VAKEVEEGED PDSFEEVLKL VLTEFERAFL RGNEVHALAA
SLPGITEKKL VTVRSYYAAR AAVERPIKHH ESALFREASD ENAFIYAVLG GQGNIEEYFD
ELREIYNTYP SFVEDFIAAE AQHLLQLSRD PRAEKLYSKG LDVMRWLNNR DSQPDTDYLV
SAPVSLPLIG LTQLAHYVVT CRVLGSHPGH VRSRLRGVTG HSQGVVTAAA IAEAKNWETF
ERAAKKAIEI LFWIGTRSQQ AFPRTSLAPT VLQDSIDNGE GTPTPMLSIR DLSRKAVQDH
IDATNAHLPK DRHIAISLVN SARNFVVTGP PISLYGLNLR LRKDKAPTGL DQTRIPFTER
KVRFVNRFLP ITAPFHSPYL ADATKQLEDD LKAIKISTAD LGIPMYDTHT GQDLRETDTD
DIVPRLVRMI TADSVEWEKA TVFPKATHIL DFGPGGISGL GVLTNRNKDG TGVRVILAGA
IDGQNAEVGY KPEIFDRDFD HAVKYAVDWV KEHGPRLVKT STGQTYVDTK MSRTLGLPPV
MVAGMTPCTV PWDFVAATMN AGYEIELAGG GYYNEKTMTA AISKVEKAIP AGRGITVNLI
YVNPRAMGWQ IPLLAKLRAD GVPIEGLTIG AGVPSIEVAN EYIETLGIKH IAFKPGSVEA
IQQTINIAKA NPTFPVLLQW TGGRGGGHHS FEDFHQPILQ MYSRLRKCDN LILVAGSGFG
GAEDTYPYLT GSWSTKFGYP PMPFDGCLFG SRVMTAKEAH TSKMAKQAIV DAPGLEDSEW
EKTYKGPAGG VITVRSEMGE PIHKLATRGV IFWHEMDQKI FSLDKAKRVP ELKKMREYII
EKLNKDFQKV WFGKNKKGMS VDLEDMTYAE VVQRMVELMY VKHQSRWIDP SLKRLTGDFI
RRLEERFSKT SNESLIQNYE ELNDPFPMLE KVFKAYPEAD DQLINAQDVQ HFLLLCQRRG
QKPVPFVPVL DDTFEFFFKK DSLWQSEDLD AVVDQDVGRT CILQGPMAVK YSTKVDEPIK
EILDGVHEGH IKYLLRDIYG DDESKVPVIE YFGSNLLAPP QGLEVDGLTI SELENKIIYR
LAAAPNATMP EVHSWLQLLA GTSYSWRHAF FTADIFVQGQ RFQTNPTARI FAPTRGMIVE
IQNPKEPAKT SIIVKELHTG GKLIKTADVS LTKDNEILLN LYEERTALKQ PVALPFRFNY
RPDVGYAPIH EVMEARNDRI KEFYYKIWFG DEACPFDASV TSRFDGGRAT VTSEAINDFV
HAVGNTGEAF VDRPGKEVFA PMDFAIVVGW KAITKPIFPR AIDGDLLKLV HLSNGFRMIS
GAEPLKKGDV LDTTAQINAV INQDSGKMVE VCGTITRDGK PVMEVTSQFL YRGAYDDFEN
TFQRKVEKPI QLHLATSKDV AILRSKEWFN FEEPEIDLLN KTLLFKLETV VRYKNKTVFS
DIETQGEVLL ELPTKEIIQI ASVDYRSGTA FGNPVMDYLE RNGAAVDQPV LFENAIPLHG
KTPLSLKAPA SNENYARVSG DYNPIHVSRV FASYANLPGT ITHGMYSSAA VRSLVETWAA
ENNVGRVRSY HVNLVGMVLP DDMLDVKLQH VGMVSGRKII KIEVSNQETE DKVLLGEAEV
EQPTTSYVFT GQGSQEQGMG MELYNSSPVA KEVWDRADKH FMDNYGFAIT NIVKNNPKEL
TIHFGGPVGK AIRQNYMSMT FETVAADGTI KSEKIFKEID ENTTSYTYRS PAGLLSATQF
TQPALTLMEK ASFEDMRAKG LIQVESTFAG HSLGEYSALA AMAEVMPIES LVSVVFYRGL
TMQVAVERDE TGRSNYSMCA VNPSRISKTF NEQALQYVVE NIAETTGWLL EIVNYNIANM
QYVAAGDLRA LDCLTGVTNY LKQQKIDIQA LMQTLSLEEV KNHLVEIIKG CAEQTEAKPK
PLDLQRGFAT IPLKGIDVPF HSTFLRSGVK PFRSFLLKKI HKTSIDPSKL VGKYIPNVTA
KPFALTKEYF EDVYKLTNSP KIGNILANWE KYEESGKEET KTEAAA
//
