ID A0A0F8UQQ6_9EURO Unreviewed; 1918 AA.
AC A0A0F8UQQ6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN ORFNames=ARAM_004341 {ECO:0000313|EMBL:KKK21818.1};
OS Aspergillus rambellii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK21818.1, ECO:0000313|Proteomes:UP000034291};
RN [1] {ECO:0000313|EMBL:KKK21818.1, ECO:0000313|Proteomes:UP000034291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK21818.1,
RC ECO:0000313|Proteomes:UP000034291};
RA Moore G.G., Beltz S.B., Mack B.M.;
RT "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT Species Obtained from the Cote d'Ivoire.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PIRNR:PIRNR005562}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKK21818.1}.
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DR EMBL; JZBS01001662; KKK21818.1; -; Genomic_DNA.
DR STRING; 308745.A0A0F8UQQ6; -.
DR OrthoDB; 2238313at2759; -.
DR Proteomes; UP000034291; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
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:InterPro.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:InterPro.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd03447; FAS_MaoC; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 2.40.128.700; -; 1.
DR Gene3D; 3.30.1120.100; -; 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; 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; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR005562};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR005562};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR005562};
KW Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1549..1852
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 145
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1687
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 1918 AA; 212031 MW; DDE32D3CE9EF0FD6 CRC64;
MRPRTPYEPS SLLGAVDTGH VHLYACCGGQ GPSNLTGLDD LIHLSLTYNH CSPIQLLLAS
AARRITSLAS IPHRSAFFCG RGFPLQAWLD DQGASAPSAE DLALSPFSFP INTLLTLVHY
ALAAHKLCLD PTQLRERLHG VVGHSQGVFA AAAIAHVGTG WPAFYQAADL ALQLAFWVGL
ESHVAAPGST LSAEEVKDCV DHEEGTASYL LSVVGMTPKD LTSVIQQLNK SQAEDGGPLV
YLALVNGRNK CVVAGAPQGL QRVCMALRNH KAPAKLDQSR VLFNRRQPVI DVQYLPISAP
YHSPFLESVE SFAMSALANL RLTGEDLAIP IYHSVDGHNL QKQGSQDVLR PLIQAVTVGY
VDWPATCRQM KGATHILALG PGAVGNLVQD VMEGTGVAII PLSGRSLSSG LSSLANWGMS
SLTAPNWRRQ YSPRLRVGAN QRTPYVETKM TRLLDTPPLM VAGMTPTTGS PEFVAAIMQA
GYHAEFAGGS YHRRAEMEVA LRRLAAAIPP HRGITCNVIY ASPKTLSWQI ELLRDLIDEG
LPIEGLTVGA GIPSLEVIRG WIESLGLCHI WFKPGSVNAI DQVIALARHY PTFPIGLQWT
GGRAGGHHSS EDFHQPILDR YTRIRECENI VLVAGSGFGG ASDTWPYLTG TWSQQLGFAA
MPFDGVLFGS RMMVAREAKT SLAAKRLIVD APGIEDDDRA TWTRSEIEPV GGVISVTSEM
GQPIHVLATR AMLLWHELDT RFFSIRDTQK YLNALQRHRE YIISRLNVDY ARPWFALTLS
GEAVEIEDMS YKDVLRRLCQ LMYVPHEARW IDLSYLHLVH GFLHLVQSRF GYGVYLSEDP
VELQATFDNA YAAQGDEVLH PEDVAHLLAL FRRRGQKPVP FIPKLDVNFE TWFKKDSLWQ
SEDVEAVPNQ DPQRVCIIHG PLAARHSTVC NEPVGHILDC IRDAHIEMLC QQREDEEEQE
EEEGTIRHET VQKKELSLPG VRVSQDGPIH RYHLIGPALP SAEALVEHLV GDCTWAYAAL
INKYLIYGQN RAKNPIRNAF RPEAGDVIDV RYAAEQPCEI TLYTAPLRGD SKHPHAVLEL
AYHEGREVTM TLLMSPILGG QSRRPALELT MQLIGGPMDS HMLQLSRGDY LDRVRRLYTQ
LWIEGPSHGP SSAGINSEFA GDRVTITADA VKAFLAVIRQ TGPARCQAWE AQGSVIPLDY
GVVLAWTVLT KPVLLPALDG DPVQLLHQSI SIRLVPGVRP LHLGDVVTTS SRITERTITA
TGQLIEVSAE IRREAEPVVH IRSVFVIQRR PQSVSKQQFR SVDEPDMIMH INSPVKLQVL
VSRKWLLLDG STPDLLGKTL VFRLNTQTIY DTSGTLSSLQ VAGSVSLLPE ITSSSSSLGA
QLGRVYLEEE GCRVNPVLDF LHRHAAPRIQ RRMLQNPGWA GDATIDFRAP SQSGSYACVS
QDTNPIHLCP LFARFAGRGA PVVHGMHLSA TVRRILEWMV GDTHRTRFRS WKTSFDGIVR
VQDQLQMEVQ HRAMEDGLLV VQVKVLDQNG QRPVMRAEAI IEQAPTAYVF CGQGSQEKGM
GMALYGTHTA AQALWDKAER HFESQYGFSL LQIVRENPTS LTVNFGGRRG RQIRANYLAM
SSGSDSDTCI LPGLTASCRS YTFSYPAGLL MSTQFAQPAL AVMEMAEYAH LQAQGVVQNP
ALFAGHSLGE YSALGACTTF MPFESLLSLI LYRGLKMQNA LPRDTYGRTD YAMMAADPSR
IRPDFDEHDF IDLVQLIGQE AGLLLEVVNH NVRSRQYVCA GHVRALWIMG RVCDELFKLT
LTGDGDTLRE CVRRHVLGSQ SVTNQTNLAR GRATIPLGGV DIPFHSQMLR GHIDNYRQYL
RRHLRISDLK PDEFVGRWIP NVVGKPFALD SSYIHLVQRV TGSQPLMDLL QRLKERLA
//