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Database: UniProt
Entry: A0A0F8UQQ6_9EURO
LinkDB: A0A0F8UQQ6_9EURO
Original site: A0A0F8UQQ6_9EURO 
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
//
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