HEXB_DOTSN
ID HEXB_DOTSN Reviewed; 1904 AA.
AC M2XHU6;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Fatty acid synthase beta subunit hexB {ECO:0000303|PubMed:23207690};
DE EC=2.3.1.86 {ECO:0000305|PubMed:23207690};
DE AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000305|PubMed:23207690};
DE EC=3.1.2.14 {ECO:0000305|PubMed:23207690};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000305|PubMed:23207690};
DE EC=4.2.1.59 {ECO:0000305|PubMed:23207690};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000305|PubMed:23207690};
DE EC=1.3.1.9 {ECO:0000305|PubMed:23207690};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000305|PubMed:23207690};
DE EC=2.3.1.38 {ECO:0000305|PubMed:23207690};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000305|PubMed:23207690};
DE EC=2.3.1.39 {ECO:0000305|PubMed:23207690};
DE AltName: Full=Dothistromin biosynthesis protein hexB {ECO:0000303|PubMed:23207690};
GN Name=hexB {ECO:0000303|PubMed:23207690}; ORFNames=DOTSEDRAFT_181128;
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990;
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 [3]
RP FUNCTION.
RX PubMed=12039746; DOI=10.1128/aem.68.6.2885-2892.2002;
RA Bradshaw R.E., Bhatnagar D., Ganley R.J., Gillman C.J., Monahan B.J.,
RA Seconi J.M.;
RT "Dothistroma pini, a forest pathogen, contains homologs of aflatoxin
RT biosynthetic pathway genes.";
RL Appl. Environ. Microbiol. 68:2885-2892(2002).
RN [4]
RP FUNCTION.
RX PubMed=16649078; DOI=10.1007/s11046-006-0240-5;
RA Bradshaw R.E., Jin H., Morgan B.S., Schwelm A., Teddy O.R., Young C.A.,
RA Zhang S.;
RT "A polyketide synthase gene required for biosynthesis of the aflatoxin-like
RT toxin, dothistromin.";
RL Mycopathologia 161:283-294(2006).
RN [5]
RP FUNCTION.
RX PubMed=17683963; DOI=10.1016/j.fgb.2007.06.005;
RA Zhang S., Schwelm A., Jin H., Collins L.J., Bradshaw R.E.;
RT "A fragmented aflatoxin-like gene cluster in the forest pathogen
RT Dothistroma septosporum.";
RL Fungal Genet. Biol. 44:1342-1354(2007).
RN [6]
RP REVIEW ON FUNCTION, AND PATHWAY.
RX PubMed=22069571; DOI=10.3390/toxins2112680;
RA Schwelm A., Bradshaw R.E.;
RT "Genetics of dothistromin biosynthesis of Dothistroma septosporum: an
RT update.";
RL Toxins 2:2680-2698(2010).
RN [7]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=23207690; DOI=10.1016/j.fgb.2012.11.006;
RA Chettri P., Ehrlich K.C., Cary J.W., Collemare J., Cox M.P.,
RA Griffiths S.A., Olson M.A., de Wit P.J., Bradshaw R.E.;
RT "Dothistromin genes at multiple separate loci are regulated by AflR.";
RL Fungal Genet. Biol. 51:12-20(2013).
RN [8]
RP FUNCTION.
RX PubMed=23448391; DOI=10.1111/nph.12161;
RA Bradshaw R.E., Slot J.C., Moore G.G., Chettri P., de Wit P.J.,
RA Ehrlich K.C., Ganley A.R., Olson M.A., Rokas A., Carbone I., Cox M.P.;
RT "Fragmentation of an aflatoxin-like gene cluster in a forest pathogen.";
RL New Phytol. 198:525-535(2013).
RN [9]
RP INDUCTION.
RX PubMed=25986547; DOI=10.1016/j.funbio.2015.01.007;
RA Chettri P., Ehrlich K.C., Bradshaw R.E.;
RT "Regulation of the aflatoxin-like toxin dothistromin by AflJ.";
RL Fungal Biol. 119:503-508(2015).
CC -!- FUNCTION: Fatty acid synthase beta subunit; part of the fragmented gene
CC cluster that mediates the biosynthesis of dothistromin (DOTH), a
CC polyketide toxin very similar in structure to the aflatoxin precursor,
CC versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571,
CC PubMed:23207690, PubMed:23448391). The first step of the pathway is the
CC conversion of acetate to norsolorinic acid (NOR) and requires the fatty
CC acid synthase subunits hexA and hexB, as well as the polyketide
CC synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a
CC hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize
CC the precursor NOR (By similarity). The hexanoyl starter unit is
CC provided to the acyl-carrier protein (ACP) domain by the fungal fatty
CC acid synthase hexA/hexB (By similarity). The second step is the
CC conversion of NOR to averantin (AVN) and requires the norsolorinic acid
CC ketoreductase nor1, which catalyzes the dehydration of norsolorinic
CC acid to form (1'S)-averantin (PubMed:23207690). The cytochrome P450
CC monooxygenase avnA then catalyzes the hydroxylation of AVN to
CC 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed
CC by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690).
CC Averufin might then be converted to hydroxyversicolorone by cypX and
CC avfA (PubMed:23207690). Hydroxyversicolorone is further converted
CC versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is
CC then the substrate for the versiconal hemiacetal acetate esterase est1
CC to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase
CC vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC ring (PubMed:16649078, PubMed:23207690). Then, the activity of the
CC versicolorin B desaturase verB leads to versicolorin A (VERA)
CC (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform
CC epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a
CC cytochrome P450, such as cypX or avnA could catalyze this step
CC (PubMed:23207690). It is also possible that another, uncharacterized,
CC cytochrome P450 enzyme is responsible for this step (PubMed:23207690).
CC Opening of the epoxide could potentially be achieved by the epoxide
CC hydrolase epoA (PubMed:23207690). However, epoA seems not to be
CC required for DOTH biosynthesis, but other epoxide hydrolases may have
CC the ability to complement this hydrolysis (PubMed:23207690).
CC Alternatively, opening of the epoxide ring could be achieved non-
CC enzymatically (PubMed:23207690). The next step is the deoxygenation of
CC ring A to yield the 5,8-dihydroxyanthraquinone which is most likely
CC catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690).
CC The last stages of DOTH biosynthesis are proposed to involve
CC hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might
CC have oxidative roles here (PubMed:23207690). An alternative possibility
CC is that cytochrome P450 monoogenases such as avnA and cypX might
CC perform these steps in addition to previously proposed steps
CC (PubMed:23207690). {ECO:0000250|UniProtKB:Q8TGA1,
CC ECO:0000269|PubMed:12039746, ECO:0000269|PubMed:16649078,
CC ECO:0000303|PubMed:22069571, ECO:0000305|PubMed:17683963,
CC ECO:0000305|PubMed:23207690, ECO:0000305|PubMed:23448391}.
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
CC -!- PATHWAY: Mycotoxin biosynthesis. {ECO:0000303|PubMed:22069571,
CC ECO:0000305|PubMed:23207690}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC -!- INDUCTION: Expression is positively regulated by the dothistromin-
CC specific transcription factors aflR and aflJ (PubMed:23207690,
CC PubMed:25986547). {ECO:0000269|PubMed:23207690,
CC ECO:0000269|PubMed:25986547}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; KB446546; EME39032.1; -; Genomic_DNA.
DR AlphaFoldDB; M2XHU6; -.
DR SMR; M2XHU6; -.
DR STRING; 675120.M2XHU6; -.
DR EnsemblFungi; EME39032; EME39032; DOTSEDRAFT_181128.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OMA; VCAGHFR; -.
DR OrthoDB; 8490at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
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:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 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 Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 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; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 2: Evidence at transcript level;
KW Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transferase.
FT CHAIN 1..1904
FT /note="Fatty acid synthase beta subunit hexB"
FT /id="PRO_0000443457"
FT DOMAIN 1399..1512
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 24..395
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000255"
FT REGION 447..691
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 1001..1491
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1530..1893
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1904 AA; 210940 MW; BBF577222C8B2732 CRC64;
MGSQHQSQHN SALIQAARDG EATLSVAFGG QGPSNLNCFN DLLELNKTYG STLRPLIHTA
DATLSELASL PHRSGFHEDE GFETLDWLQD PKQAPSREYL ALSPMSFPIN TLLSLCNYCV
TLRALRLDPG QFRSSLHNVV GHSQGIFAAA AIAKADSWES FLEAAEIALK ISFWVGLESH
TAAPPSHISA AAVQDCVEHG EGQPSSMLGI TGLNRAQVEM LVERVNKSLS DDDRHVCLAL
ANSRDKYTIA GPPHSLRAVC VQIREIRAAD GVDQSRILFN KRKQEVDALF LPISAPYHSQ
YLKQVSNNVL DALDVDLVGS ELGIPLLHTQ SGQNLQDWKS KSIIKAIVCA VTTDMVEWPD
VCQRLGSSYI LGFGPGNIGN LIHESTEGTG VRVIQMNDRS PGSRGIGARA ELFSEEMPPQ
ALDWKQTFGP RLVLDHRGDV QIQTRMTQLL NAPPVMVAGM TPTTVTWDFV SCVMQAGYHV
ELAGGGYSSE ARFEEALRRL AASIPIYRGI TCNLLYANPQ TIAWQVAVLR RLIKEGISIE
GVTIGAGVPS PDVIKEYIAI GLKHISFKPG SIAAIDEVIE IAQAHPQFPI GLQWTGGRAG
GHHSHEDLHL PILKTYARIR RCSNIVLIAG SGFGGGSDTY PYISGDWSKS LSYPPMPFDG
ILLGSRVMVA KEAHTSPQAK QLIVQTEGVG DNDWHTSFET PTGGVITITS EHGQPIHMLA
TRGVMLWKEF DKRIFSIKDA AKRLSYIRAH REEIITRLNK DYQKPWFGVN GDGQNVDLDR
MTYREVLGRM CQLMSRGDNG WTDPSWLAMV KDFVEIAGER FGCQVDAHAT KAPEVRTAFE
ATLGGSVDET LYPEDVALVL ELLRRRGRKP PPFVPALDEN FETWCKKDSL WQSEDVDSLV
GKDVQRACII QGPVAVRHST IHDEPVQDIL DNICNFHIES LLQSGETPGV ARKQDLGRPN
SIKKSVPGVQ ITTEKTTIRY QVHKTDKLPP EMDTLIEHIV GPAADCWTHH CLKDEWVFRD
QARLRNPIRA AFLRQIQPGE VIEVRLSRDG NTQAIALKTA LFGKSSLQTV LRIASTDGKS
IKVALTPPSF LSDKPLGLQF AYQLSRKSRG SKLVEVTPNR LDAIKGFYAQ LWVDSNQDVK
EAGLNSEFWG EPTTLLAQDV QNYTAVVSRS TSPQLQAWNP TGSVPVDYCI VLAWTALTKP
LTIPALQCDL LNLLHRSVNF KYAANARPLR LGDVTQTVSR ITSLTIQPTG KLVEVSAELR
RNDETVVTIT TEFFIVGQFE DYETQFKSFE EPLFEVRVHS VTRQALLQSR KWLVLDDPSM
DLAGLTLAFK LNTHTTFDHE GKVGALQVTG SVSRVESTGF DTRIGKVYFK KDSCNGNPVV
DFLNRHGYPR VTRQPLENPG WNEGSTVLMK APAKSNQYAM ASKDTNPLHV CGVFARYAGL
PDTVVHGMHT SAIVRRAVEW AVGDSDRSRF KKWQVSFEGM VRPNDRLKIQ LQHTAMEHGR
MIMKVQAFND ETGDKVIEAE AEVEQPRTGY VFCGQGSQEK GMGMSLYNAR PEAKALWDRG
DQFLREQYGF SLLSLVRENP TTLTINFGGR RGKRIRDNYL AMTKKTSLKA DAKDVCIVQG
LTPTSTSHTF SETKGLLFST QFSQPAIALM EMVEHEHLFA KGVVQPSALF AGHSLGEYAA
LGACTTFMPF ESLLTLIFYR GLKMQNALER DANGRTDYSM MAADPSRVGK AGFDERAFQC
LVELVNEETG LLMEIVNHNV RSQQYVCAGH FRALWILGKV CDDLAKHPKI HLLSMQDLKD
MVTTHVPAAG KLTNDIVLTR GKATIPLNGI DIPFHSTMLR GEIEHFRRYL LTKVNVPDIK
PNELVGKWIP NVVGRPFSLD RSYIEHVQSV TGSEPLQKML KAMA
