ID H1VYE2_COLHI Unreviewed; 2100 AA.
AC H1VYE2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Acyl transferase {ECO:0000313|EMBL:CCF45254.1};
GN ORFNames=CH063_00548 {ECO:0000313|EMBL:CCF45254.1}, CH63R_13998
GN {ECO:0000313|EMBL:OBR02772.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF45254.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|EMBL:CCF45254.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF45254.1};
RA Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
RN [3] {ECO:0000313|EMBL:OBR02772.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR02772.1};
RA O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000092177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA Thon M.R., O'Connell R.J.;
RT "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT structure and association of transposable elements with secondary
RT metabolite gene clusters.";
RL BMC Genomics 18:667-667(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 -!- 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; CACQ02007568; CCF45254.1; -; Genomic_DNA.
DR EMBL; LTAN01000010; OBR02772.1; -; Genomic_DNA.
DR RefSeq; XP_018151290.1; XM_018308972.1.
DR STRING; 759273.H1VYE2; -.
DR EnsemblFungi; CCF45254; CCF45254; CH063_00548.
DR GeneID; 28873079; -.
DR KEGG; chig:CH63R_13998; -.
DR VEuPathDB; FungiDB:CH63R_13998; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR Proteomes; UP000092177; Chromosome 10.
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; 6.10.60.10; -; 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; SSF51395; FMN-linked oxidoreductases; 1.
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 Transferase {ECO:0000256|PIRNR:PIRNR005562, ECO:0000313|EMBL:CCF45254.1}.
FT DOMAIN 1697..2016
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..20
FT /note="Disordered"
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 1841
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2100 AA; 232767 MW; 163B81422926878E CRC64;
MYGAGTGPQT GVSTPRSNAS LRPLTLRHGS LETSLLVPTA LHFHASQLKD RFNATLPTAT
DELAQDDEPS SVAELVARYM GFVADEVEKG EDDESGSYEE VLKLVLNEFE RGYLQGNEVH
ALAATLPGID AKKLVVIRSY YQARQTTGRS IKAYGSALFR AADDGSADIY TIFGGQGNIE
EYFDELREIY KTYQPFIGEL ILNAAELLQT LSKHPEAEKL YPKGLDIMRW LESEDETPDV
DYLISAPVSF PLIGLVQLAH YEVTCKVLGV HPGLLRDQIS GTTGHSQGIV LAAITAAAES
WESWKELAPS ALTILFWIGA RSQQVFPRTS LTPTMLRESV DNGEGLPTPM LSIRDLSQAE
VQKHIDATNK YLPADRHISI SLINSPRNLV VTGPPISLYG LNAQLRKVKA PTGLDQNRIP
HAQRKLRFVH RFLPITAPFH SKYLAEATEL IDEDLKNIKI PSKALGTAVF DTNTGKDLRE
AGDSNIVPTI VRLITRDPVN WEKATVFPQA THVLDFGPGG ISGLGVLTSR NKEGTGVHVI
LAGAVDGSIT EVGYKPELFD RDEEHAVKYA VDWVKEFGPR LVTNSNGDTY VDTKMSRLLG
LPPIVVAGMT PCTVPWDFVA ATMNAGYHIE LAGGGYFDPG MMTAALKKIE GAIPAGRGIG
VNLIYVNPRA MQWQIPMLGR LRAEGVPIEG LTIGAGVPSV EVAQEYIDTL GLKHISFKPG
SVDAIQAVVN IAKANPTFPV ILQWTGGRGG GHHSYEDFHQ PILTMYPRIR RQANIILVAG
SGFGGAEDTY PYLTGEWSRN YGYPPMPFDG TLFGSRMMVA KEAKTSPAAK QAIIDAPGVD
DSEWEKSYTG PTGGVITVLS EMGEPIHKLA TRGVLFWAEM DKKIFSLPKE KRVPELKKNR
DYIIKKLNDD FQKVWFGRNR AGEAVDLEDM TYGEVVRRMV DLLYIRHEQR WIDPTFIRLT
GDFIRRVEER FTSTPGQVAQ LQDFKDLQSP YETVEKILSH YPDAETQLIN AQDVQHFLML
CLRPIQKPVT FIPTLDENFD FYFKKDSLWQ SEDLGAVIGQ DVGRTCILQG PTAVKFSKVI
DEPIKDILDG IHLTHVEYLT RDLYKGDKKA IPTIEYFGGK LIETDIPVED VDGLTVSYDD
AHKNTYRLST SPTATLPSLD AWLALLAGPD RSWRHALLTS EVVVQGQKFQ TNPLKRIFAP
ARGLFVEIQN PKDPKKTKII VKEQPRHNQY VDVIEVKLEG QNDIVVNMIK DTTALGKPVA
LPLKFTYHPE AGYAPIREVM EGRNDRIKEF YWRAWFGDEK FDLDADVSSK FDGGKATITG
EDINDFIHAV GNTGEAFVER PGKTVYAPMD FAIVVGWKAI TKPIFPRTID GDLLKLVHLS
NEFRMKPGAE PLKKGDEVST TAQINAVINQ ESGKMVEVCG TIYRDGEAVM DVTSQFLYRG
AYTDYENTFQ RKMETPIQLH LATSKDVAVL KSKQWFNTDD LPRDLDLLGQ TLTFRLQSFY
RYKTKTMYSS VSTQGQVLLE LPTKEVIQVA SVDYEAGQSN GNPVVDYLER NGTPLDQPLH
FENPIPLSGR TPLQLRAPAT NENYARVSGD YNPIHVSRVF ANYAALPGTI THGMYSSAAV
RSLVETWAAE NNIGRVRSFH ASLVGMVLPN DDLQVKLQHV GMVSGRKIIK VEASNKETEE
KVLLGEAEVE QPVTAYVFTG QGSQEQGMGM ELYASSEVAR EVWDRADKYL LDNYGFSITN
IVKNNPKELT VHFGGPRGKA IRQNYMAMTF ETVSADGTIK SERIFKEIDE KTTSYTYRSP
TGLLSATQFT QPALTLMEKA SFEDMKSKGL VPRDCTFAGH SLGEYSALAA LAEVMPIESL
VSVVFYRGLT MQVAVERDAA GRSNYSMCAI NPSRISKTFN EEALQFVVDC ISEETGWLLE
IVNYNIANMQ YVAAGDLRAL DTLTGVTNFL KQQKIDIEEM RGNIDEAKGA LKEIIKGSAE
ATLKKPTPLE LQRGFATIPL RGIDVPFHST FLRSGVKPFR SFLLKKINKT TIDPAKLVGK
YIPNVTAKPF AITKEYFEDV YKLTNSPKIA SILANWDQYT QDGPAATAVN GEHEGPGAAA
//
