ID A0A1R3RIB8_ASPC5 Unreviewed; 2107 AA.
AC A0A1R3RIB8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
DE Flags: Fragment;
GN ORFNames=ASPCADRAFT_149510 {ECO:0000313|EMBL:OOF94221.1};
OS Aspergillus carbonarius (strain ITEM 5010).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=602072 {ECO:0000313|EMBL:OOF94221.1, ECO:0000313|Proteomes:UP000188318};
RN [1] {ECO:0000313|Proteomes:UP000188318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 5010 {ECO:0000313|Proteomes:UP000188318};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(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 -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000256|ARBA:ARBA00033756}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000256|ARBA:ARBA00010009}.
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DR EMBL; KV907502; OOF94221.1; -; Genomic_DNA.
DR STRING; 602072.A0A1R3RIB8; -.
DR VEuPathDB; FungiDB:ASPCADRAFT_149510; -.
DR OrthoDB; 2417129at2759; -.
DR Proteomes; UP000188318; 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: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-EC.
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; 2.40.128.700; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
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; 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; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000188318};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1726..2053
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 52..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1870
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT NON_TER 2107
FT /evidence="ECO:0000313|EMBL:OOF94221.1"
SQ SEQUENCE 2107 AA; 232822 MW; 30473BA459BACD44 CRC64;
MSRATSVSAG CRTLRCEISL RRSEPRRAGS PAPTAPHLRS HMYIPASRHE KMLQPPSAMS
THPSTPSYVD LGSPPSKPDD EIDHLVPFAL AFNALDYVSR VPAHLQVVLE NQKHRFLESL
VSEPPVSTVT LVLSFLQHLV DVDTDSETVR CLLQAFSRDF LASTDIHTLV AALPEPLPTQ
KRLLRAFYAA THHAAWSPSV PRSALLADAE RGLRLVAVFG GQGASNPRCV QELQELYTVY
APLLTPLIDV LDRELTDLCR HPDTVAFYHG RSIQLRKWLD RPGSVPDPAY IQTAAVSFPI
IGAIGLAHFA ITCHVLDHTP GQVRSLLHGV TGHSQGIVVA AGIARSDSWA SFYENAQLAV
RTLFWLGYES QQAPTAREPV SASLVEECRA HGEGAPSTML HIGGLSKSQV IQIIDQSNRE
LVAHHQVYLA LSNTQESFVV AGPPRALVGV HRRLRELKAD PARDQSRIPF DRRKPVVNHQ
FLPISAPFHT PYLQQTARAV KDRLSGSRFP ATELRSPVYH TRDGSVLTGD IDAIASLVDA
VLTDPVDWPA TVQFPSGTCV LAFGKGVAEM LARNLEGRGV GIVDSTQLTP GKAASGARPD
IFAAHLPRTL VPPSWEEEFR PRLIQAKTGE MRIVTKLTAV LGAPPVIVAG MTPTTVPWDF
VAAIMNAGYH AELAGGGYYN ADSMEQAITT LAANIPPGRG ITCNLIYASP KALGWQIALL
RRLAQPGPSP VEGLTIGAGI PSSEVASEYI TTLGLRHITF KPGSETAIDQ VLEIAKAHAD
FPIIIQWTGG RAGGHHSFED FHGPILRKYG AIRACNNVSL IGGGGFGEAQ QVYPYLSGSW
SVPHGYAPMP FDGILLGSRV MVAQEAHTSP QAKQLICATP GVAADSQWTQ SYVRPAGGIV
TVQSEMGQPI HKLATRGVLF WKEMDEQIFS LPRDKQLGAL QKRKNHIIQR LNADYFRPWF
GKKATGEPVE LEEMTYQEVL ERLVDVMYLR GQARWVHPSY TRLVIDVAMR SLERLQQAPV
DGVITPATLT RDPLGFLADL RHIVPQASST LLHPEDRSWF LQRCRVPGQK PVNFIPVLDQ
DFAVWFKKDS LWQSEDVDAV PDQDADRICI LHGPVAARYA HRIDEPVKEI LDGMIAPLAE
MLEAEFYREA PIPMTEVDTS SVHHRRLRNI LHVVEEEPGV FTYQPLPGKE LPPADQWLAY
LAHETTGWMR AIVSNQVLRR GPGRRPNWLR DCLILTWDTV ITINQSQSTL LVTRDEDGDT
YPVVSMTSTD GNRVLVQVYH RAPRSDTPIP LELQFLYNAE GGTLSEVQDQ HDARVQSFYH
KLWLGKNPPS IAANGTYYGG QKILTADLRD AWTSVVGLSY PNQRDLSAEG NDIPIHAAMV
PAWEALVAPL VTPHHEGDLL QLVHLSNSFQ LEPGESPLQI GDIVEVSASV QAVVVDDRGK
EIQVVAELKR EDRRAMTITS AFFIRGAFTD SHECFRTIDE PEILLHKLTA VDDAILRDRA
WLHVDDSIPL IGETLSFQLH THERWTKSSP TRRNIQTTGD VYKLGPRPGT RVRVGEVRFQ
APSTPGNPVL DFLTRKGQKA LVRQELTQPG WPGPTNSQTV QMPASSERYS QISIDSNPIH
TAPTFVRIAQ LPGTIVHGMY TSAVAGSVLE HLIDGWDPRR LRRWAVRFVG MVHQGDKVTV
RCRHIAMLEG RIVLEIQAFR QGEDGQDEEK VLDGEAEIEQ PATAYVFTGQ GSQSPGMGMD
IYRSSPVARQ IWDEMDEYFR DNYGFSILQI VQDNPKELTI HFGGPHGRRI RERYQAMRVD
SVSPDGQLIS KPVLPGLTSA TRSHTFHEPR GLIYSTQFAQ PAITILEKAI FEEMRARGLI
QDGAPFAGHS LGEYGALAAI AEFMPFPSFM DVVFYRGLAM QLAMERDEAG TTDYSMVAVN
PRRVGPTVTE TAIRRITSMI AQQSNRLLEI VNLNVSGEQY VCAGHLRNIH TLTSVLNELA
QSTPERLTCC LNEITPPNEP HPNPSSTLLH QSITRALTAA ESIPKPIPLI RGAATIPLTG
IDVPFHSSML RSGVDGYRRF LQARVREADV QPDILERGYI PNVTGRAFRL DRGYVEEVVR
LTGSEVL
//
