ID A0A0C4DP87_MAGP6 Unreviewed; 2112 AA.
AC A0A0C4DP87;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Fatty acid synthase beta subunit dehydratase {ECO:0000313|EMBL:KLU82571.1};
GN ORFNames=MAPG_01643 {ECO:0000313|EMBL:KLU82571.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_01643T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|EMBL:KLU82571.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82571.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU82571.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82571.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_01643T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_01643T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_01643T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_01643T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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 -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000256|ARBA:ARBA00010009, ECO:0000256|PIRNR:PIRNR005562}.
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DR EMBL; ADBL01000401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876966; KLU82571.1; -; Genomic_DNA.
DR STRING; 644358.A0A0C4DP87; -.
DR EnsemblFungi; MAPG_01643T0; MAPG_01643T0; MAPG_01643.
DR VEuPathDB; FungiDB:MAPG_01643; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR OMA; HFMDNYG; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000011715; 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; 3.30.70.2430; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.250.1850; -; 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:UP000011715};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1692..1992
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2082..2112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1836
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2112 AA; 234772 MW; 96711DF65512E046 CRC64;
MYGTGTGAHT GATTPRSSSS LRPLNIAHGS LETSFLIPTN LHFHASQLKD RFSTSLPAPT
DELAQDDEPS SVPELVARYM GFVAREVEEG EDDAQGSYEE VLKLVLNEFE RVYLRGNEVH
ALVATLPGID AKKLVVIRSY FAARYVLNRA IKPHPSALFR ASADGTAKLY TIFGGQGNIE
EYFEELRELN TTYPVFVGEL ITTSAELLRN LSSHPSAEKL FSKGLDVMTW LQHPDSTPDV
DYLISAPVSF PLIGLVQLAH YEVTCRVLGI HPGLLRERLS GATGHSQGIV LAAATAAASS
WENWAEIVKS SLTILFWIGA RSQQTFPRTS MTPSMLQDSL DNGEGMPTPM LSIRDLPQAE
VQKHIDKTNE YLPADRHISI SLINSPRNMV VTGPPISLYG LNLQLRKVRA PTGLDQNRIP
FTERKVRFVN RFLPITAPFH SKYLADATAM IDEDLQYTHL DVKNLGFPVF DTHTGKDIRE
EVKGNIVPTL VRLITRDTVN WERATVFPGA THVLDFGPGG ISGLGILTSR NKDGTGVRVI
LAGSVAGTVT EVGYKPELFD RDEEHAVKFA VDWVKEYGPK LVKTSSGRTY VDTKMSRMLG
LPPVMVAGMT PCTVPWDFVA ATMNAGYHIE LAGGGYFEPR MMQDAILKIE KAIPAGRGIS
VNLIYVNPRA MQWQIPLLGR LRAEGVPLEG LTIGAGVPSI EVANEYIQTL GLKHISFKPG
STDAIQAVIN IAKANPTFPV MLQWTGGRGG GHHSFEDFHQ PILQMYTRLR KCDNLILVAG
SGFGGAEDTY PYITGEWSKK FGYPPMPFDG CLFGSRMMVS KEAHTAPAAK KAIVDAPGVA
DDEWEKTYKG VAGGVTTVRS EMGEPIHKLA TRGVRFWAEM DQKIFSLPKE KRVAELKKNR
DYIIERLNKD FQKVWFGKNK AGQAVDLEDM TYGEVVRRMV ELMYVKHESR WIDVTYMRLT
GDFIHRVEER FVPSPGQPSL LQSYSDLQDP FPTVERILAH YPEAESQLIN AQDVQHFLQL
CMRPIQKPVV FVPTFDDDFE FYFKKDSLWQ SEDLEAVMDQ DVERTCILQG PTAVRYSKVV
DEPIKSILDG IHEGHIKGLT KDLYGSEPIP SVEYFGGKLV EPEITPDVDG LTVSYDETKN
IYRISNSPTS PMPTTEAWLS LLAGPTRCWR HAMLMSEVFV QGTKYYSNPM RRIFAPVRGL
FVEIRNPKNP AKTEIIVREQ PRHNHYVDVL LINMVSDNEI VVKMIKETTA LGKPVSLPLR
FIYKPEAGYA PIHEVMEDRN DRIKEFYWRA WFGNETLDLD AAVDGTFDGG KAVVTSEDIN
DFVHAVGNKG EAFVDRPGKV MYAPMDFAIV LGWKAITKPI FPRKIDGDLL NLVHLSNQFR
MMPGAEPLKK GDEVSTVSRV NAVVIQDSGK MVEVCGTISR DNHAVMEVTS QFLYRGVYTD
FENTFQRKVE TPMQIHLATS KDVAILKSKE WFVLDDGVDM ELLGQTLTFR LQSLVRFKNK
TVFSSVLTRG EVLVELPTKE TVQVASVEYE AGTSHGNPVI DYLERNGASI EQPINFENPI
PLSGKTPLEL RAPASNETYA RVSGDYNPIH VSRIFANYAN LPGTITHGMY SSAAVRSLVE
TWAAENNVGR VRSFHASLVG MVLPNDALQV KLQHVGMVAG RKIIKVEVLN KESEEKVLLG
EAEVEQPATA YVFTGQGSQE QGMGMDLYDS SPVAKEVWDR ADKYLMDTYG FAITNIVKNN
PKELTIHFGG PRGKAIRANY MAMTFETVAA DGSIKSERIF KDINEATSSY TYRSPTGLLS
ATQFTQPALT LMEKASFEDM KAKGLVPRDS TFAGHSLGEY SALAALADVM PIESLVSVVF
YRGLTMQVAV ERDASGRSNY SMCAVNPSRI SRTFNEEALR FVVGNIAEET GWLLEIVNYN
IANMQYVCAG DLRALDTLTG VLNFLKQQKL DIEEMKKTMK VEDVKESLQQ IIQGCAQQTE
AKPKPLDLQR GFATIPLRGI DVPFHSTFLR SGVKPFRSFL LKKINKTTID PSKLLGKYIP
NVTAKPFALT KEYFEDVYRL TNSPRISAIL ANWEKYQDDN AVPSSIMSGE TNGANGASNG
STSHNESVPA SE
//
