AFLB_ASPPU
ID AFLB_ASPPU Reviewed; 1888 AA.
AC Q8TGA1; A0A0F0I0T2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Fatty acid synthase beta subunit aflB {ECO:0000303|PubMed:16256699};
DE EC=2.3.1.86 {ECO:0000305|PubMed:16256699};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000305|PubMed:16256699};
DE EC=4.2.1.59 {ECO:0000305|PubMed:16256699};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000305|PubMed:16256699};
DE EC=1.3.1.9 {ECO:0000305|PubMed:16256699};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000305|PubMed:16256699};
DE EC=2.3.1.38 {ECO:0000305|PubMed:16256699};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000305|PubMed:16256699};
DE EC=2.3.1.39 {ECO:0000305|PubMed:16256699};
DE Includes:
DE RecName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000305|PubMed:16256699};
DE EC=3.1.2.14 {ECO:0000305|PubMed:16256699};
DE AltName: Full=Aflatoxin biosynthesis protein B {ECO:0000303|PubMed:15006741};
GN Name=aflB {ECO:0000303|PubMed:15006741};
GN Synonyms=fas-1 {ECO:0000303|PubMed:15094053},
GN fas-1A {ECO:0000303|PubMed:8572694}, uvm8 {ECO:0000303|PubMed:8572694};
GN ORFNames=P875_00052979;
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=16256699; DOI=10.1006/bioo.2001.1216;
RA Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
RA Townsend C.A.;
RT "Hexanoate synthase, a specialized type I fatty acid synthase in aflatoxin
RT B1 biosynthesis.";
RL Bioorg. Chem. 29:293-307(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND NOMENCLATURE.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15006741; DOI=10.1128/aem.70.3.1253-1262.2004;
RA Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D., Cleveland T.E.,
RA Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
RT "Clustered pathway genes in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 70:1253-1262(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RX PubMed=15094053; DOI=10.1016/s0014-5793(04)00327-8;
RA Yu J., Bhatnagar D., Cleveland T.E.;
RT "Completed sequence of aflatoxin pathway gene cluster in Aspergillus
RT parasiticus.";
RL FEBS Lett. 564:126-130(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=1339261; DOI=10.1128/aem.58.11.3527-3537.1992;
RA Skory C.D., Chang P.K., Cary J., Linz J.E.;
RT "Isolation and characterization of a gene from Aspergillus parasiticus
RT associated with the conversion of versicolorin A to sterigmatocystin in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 58:3527-3537(1992).
RN [6]
RP FUNCTION.
RX PubMed=8434913; DOI=10.1128/aem.59.2.479-484.1993;
RA Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
RA Ullah A.H.J.;
RT "Purification of a 40-kilodalton methyltransferase active in the aflatoxin
RT biosynthetic pathway.";
RL Appl. Environ. Microbiol. 59:479-484(1993).
RN [7]
RP FUNCTION.
RX PubMed=8368836; DOI=10.1128/aem.59.8.2486-2492.1993;
RA Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: conversion of norsolorinic
RT acid to averufin.";
RL Appl. Environ. Microbiol. 59:2486-2492(1993).
RN [8]
RP FUNCTION.
RX PubMed=8368837; DOI=10.1128/aem.59.8.2493-2500.1993;
RA Yabe K., Hamasaki T.;
RT "Stereochemistry during aflatoxin biosynthesis: cyclase reaction in the
RT conversion of versiconal to versicolorin B and racemization of versiconal
RT hemiacetal acetate.";
RL Appl. Environ. Microbiol. 59:2493-2500(1993).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8572694; DOI=10.1128/aem.62.1.191-195.1996;
RA Mahanti N., Bhatnagar D., Cary J.W., Joubran J., Linz J.E.;
RT "Structure and function of fas-1A, a gene encoding a putative fatty acid
RT synthetase directly involved in aflatoxin biosynthesis in Aspergillus
RT parasiticus.";
RL Appl. Environ. Microbiol. 62:191-195(1996).
RN [10]
RP FUNCTION.
RX PubMed=10543813; DOI=10.1128/aem.65.11.4987-4994.1999;
RA Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
RT "Cloning and characterization of the O-methyltransferase I gene (dmtA) from
RT Aspergillus parasiticus associated with the conversions of
RT demethylsterigmatocystin to sterigmatocystin and
RT dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in aflatoxin
RT biosynthesis.";
RL Appl. Environ. Microbiol. 65:4987-4994(1999).
RN [11]
RP FUNCTION.
RX PubMed=10584035; DOI=10.1128/aem.65.12.5639-5641.1999;
RA Zhou R., Linz J.E.;
RT "Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
RT Aspergillus parasiticus.";
RL Appl. Environ. Microbiol. 65:5639-5641(1999).
RN [12]
RP FUNCTION.
RX PubMed=11055914; DOI=10.1128/aem.66.11.4715-4719.2000;
RA Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G., Bhatnagar D.,
RA Cleveland T.E.;
RT "adhA in Aspergillus parasiticus is involved in conversion of 5'-
RT hydroxyaverantin to averufin.";
RL Appl. Environ. Microbiol. 66:4715-4719(2000).
RN [13]
RP FUNCTION.
RX PubMed=11996570; DOI=10.1021/ja012185v;
RA Udwary D.W., Casillas L.K., Townsend C.A.;
RT "Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
RT cytochrome P-450 in the final step of aflatoxin biosynthesis.";
RL J. Am. Chem. Soc. 124:5294-5303(2002).
RN [14]
RP FUNCTION.
RX PubMed=15528514; DOI=10.1128/aem.70.11.6518-6524.2004;
RA Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
RT "Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
RT formation.";
RL Appl. Environ. Microbiol. 70:6518-6524(2004).
RN [15]
RP FUNCTION.
RX PubMed=15932995; DOI=10.1128/aem.71.6.2999-3006.2005;
RA Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K., Nakajima H.;
RT "Aspergillus parasiticus cyclase catalyzes two dehydration steps in
RT aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 71:2999-3006(2005).
RN [16]
RP FUNCTION.
RX PubMed=16332900; DOI=10.1128/aem.71.12.8963-8965.2005;
RA Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
RT "An aflatoxin biosynthesis cluster gene encodes a novel oxidase required
RT for conversion of versicolorin a to sterigmatocystin.";
RL Appl. Environ. Microbiol. 71:8963-8965(2005).
RN [17]
RP FUNCTION.
RX PubMed=15771506; DOI=10.1021/ja0455188;
RA Henry K.M., Townsend C.A.;
RT "Ordering the reductive and cytochrome P450 oxidative steps in
RT demethylsterigmatocystin formation yields general insights into the
RT biosynthesis of aflatoxin and related fungal metabolites.";
RL J. Am. Chem. Soc. 127:3724-3733(2005).
RN [18]
RP FUNCTION.
RX PubMed=16461654; DOI=10.1128/aem.72.2.1096-1101.2006;
RA Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
RT "The aflatoxin biosynthesis cluster gene, aflX, encodes an oxidoreductase
RT involved in conversion of versicolorin A to demethylsterigmatocystin.";
RL Appl. Environ. Microbiol. 72:1096-1101(2006).
RN [19]
RP FUNCTION.
RX PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
RA Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y., Adachi Y.,
RA Nakajima H., Yabe K.;
RT "Involvement of the nadA gene in formation of G-group aflatoxins in
RT Aspergillus parasiticus.";
RL Fungal Genet. Biol. 45:1081-1093(2008).
RN [20]
RP FUNCTION.
RX PubMed=18403714; DOI=10.1126/science.1154711;
RA Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L., Kelleher N.L.,
RA Townsend C.A.;
RT "Deconstruction of iterative multidomain polyketide synthase function.";
RL Science 320:243-246(2008).
RN [21]
RP INDUCTION.
RX PubMed=23281343; DOI=10.1002/mbo3.63;
RA Hong S.Y., Roze L.V., Wee J., Linz J.E.;
RT "Evidence that a transcription factor regulatory network coordinates
RT oxidative stress response and secondary metabolism in aspergilli.";
RL MicrobiologyOpen 2:144-160(2013).
CC -!- FUNCTION: Fatty acid synthase beta subunit; part of the gene cluster
CC that mediates the biosynthesis of aflatoxins, a group of polyketide-
CC derived furanocoumarins, and part of the most toxic and carcinogenic
CC compounds among the known mycotoxins (PubMed:15006741). The four major
CC aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin
CC B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2)
CC (PubMed:15006741, PubMed:15094053). The first step of the pathway is
CC the conversion of acetate to norsolorinic acid (NOR) and requires the
CC fatty acid synthase subunits aflA and aflB, as well as the PKS aflC
CC (PubMed:15006741, PubMed:8572694). AflC combines a hexanoyl starter
CC unit and 7 malonyl-CoA extender units to synthesize the precursor NOR
CC (PubMed:18403714). The hexanoyl starter unit is provided to the acyl-
CC carrier protein (ACP) domain by the fungal fatty acid synthase
CC aflA/aflB (PubMed:16256699). The second step is the conversion of NOR
CC to averantin (AVN) and requires the norsolorinic acid ketoreductase
CC aflD, which catalyzes the dehydration of norsolorinic acid to form
CC (1'S)-averantin (PubMed:10584035). The norsolorinic acid reductases
CC aflE and aflF may also play a role in the conversion of NOR to AVN
CC (PubMed:15006741). The cytochrome P450 monooxygenase aflG then
CC catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN)
CC (PubMed:8368836). The next step is performed by the 5'-hydroxyaverantin
CC dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which
CC is further converted to averufin (AVF) by aflK that plays a dual role
CC in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion
CC of 5'-oxoaverantin, as well as a versicolorin B synthase in a later
CC step in the pathway (PubMed:15006741, PubMed:11055914,
CC PubMed:15932995). The averufin oxidase aflI catalyzes the conversion of
CC AVF to versiconal hemiacetal acetate (VHA) (PubMed:15006741). VHA is
CC then the substrate for the versiconal hemiacetal acetate esterase aflJ
CC to yield versiconal (VAL) (PubMed:15006741). Versicolorin B synthase
CC aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran
CC ring of aflatoxin which is required for DNA-binding, thus giving to
CC aflatoxin its activity as a mutagen (PubMed:15006741, PubMed:8368837,
CC PubMed:15932995). Then, the activity of the versicolorin B desaturase
CC aflL leads to versicolorin A (VERA) (PubMed:15006741, PubMed:8368837).
CC A branch point starts from VERB since it can also be converted to
CC dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA
CC being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins
CC B2 and G2 (PubMed:15006741). Next, the versicolorin reductase aflM and
CC the cytochrome P450 monooxygenase aflN are involved in conversion of
CC VERA to demethylsterigmatocystin (DMST) (PubMed:15006741,
CC PubMed:1339261, PubMed:15771506). AflX and aflY seem also involved in
CC this step, through probable aflX-mediated epoxide ring-opening step
CC following versicolorin A oxidation and aflY-mediated Baeyer-Villiger
CC oxidation required for the formation of the xanthone ring
CC (PubMed:16332900, PubMed:16461654). The methyltransferase aflO then
CC leads to the modification of DMST to sterigmatocystin (ST), and of
CC DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both ST and
CC DHST are then substrates of the O-methyltransferase aflP to yield O-
CC methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin
CC (DHOMST), respectively (PubMed:8434913). Finally OMST is converted to
CC aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the
CC action of several enzymes including O-methylsterigmatocystin
CC oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also
CC the NADH-dependent flavin oxidoreductase nadA which is specifically
CC required for the synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
CC PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
CC ECO:0000269|PubMed:10584035, ECO:0000269|PubMed:11055914,
CC ECO:0000269|PubMed:11996570, ECO:0000269|PubMed:1339261,
CC ECO:0000269|PubMed:15528514, ECO:0000269|PubMed:15771506,
CC ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:16256699,
CC ECO:0000269|PubMed:16332900, ECO:0000269|PubMed:16461654,
CC ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
CC ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
CC ECO:0000269|PubMed:8434913, ECO:0000269|PubMed:8572694,
CC ECO:0000305|PubMed:15006741, ECO:0000305|PubMed:15094053}.
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:0000305|PubMed:16256699};
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:0000305|PubMed:16256699};
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:0000305|PubMed:16256699};
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:0000305|PubMed:16256699};
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:0000305|PubMed:16256699};
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:0000305|PubMed:16256699};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:15006741, ECO:0000269|PubMed:15094053,
CC ECO:0000269|PubMed:16256699}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC -!- INDUCTION: Expression is regulated by the atfB, srrA, AP-1, and msnA
CC transcription regulators (PubMed:23281343). These factors bind
CC respectively to the conserved motifs CRE1 (5'-TGACATAA-3'), SRRA (5'-
CC T/GNT/CAAGCCNNG/AA/GC/ANT/C-3'), AP-1 (5'-TGAGTAC-3') and STRE (5'-
CC CCCCT-3'), present in the promoter of aflB (PubMed:23281343).
CC {ECO:0000269|PubMed:23281343}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of norsolorinic acid and
CC aflatoxin B1 (PubMed:8572694). {ECO:0000269|PubMed:8572694}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KJK60796.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF391094; AAL99899.1; -; Genomic_DNA.
DR EMBL; AY371490; AAS66003.1; -; Genomic_DNA.
DR EMBL; JZEE01000728; KJK60796.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q8TGA1; -.
DR SMR; Q8TGA1; -.
DR STRING; 1403190.Q8TGA1; -.
DR PRIDE; Q8TGA1; -.
DR EnsemblFungi; KJK60796; KJK60796; P875_00052979.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000033540; 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:0045122; P:aflatoxin biosynthetic process; IMP:GO_Central.
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 Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1888
FT /note="Fatty acid synthase beta subunit aflB"
FT /id="PRO_0000438337"
FT DOMAIN 1399..1500
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 23..395
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16256699"
FT REGION 437..682
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16256699"
FT REGION 990..1478
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16256699"
FT REGION 1517..1877
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16256699"
SQ SEQUENCE 1888 AA; 210430 MW; EC232BC88FA5F05C CRC64;
MGSVSREHES IPIQAAQRGA ARICAAFGGQ GSNNLDVLKG LLELYKRYGP DLDELLDVAS
NTLSQLASSP AAIDVHEPWG FDLRQWLTTP EVAPSKEILA LPPRSFPLNT LLSLALYCAT
CRELELDPGQ FRSLLHSSTG HSQGILAAVA ITQAESWPTF YDACRTVLQI SFWIGLEAYL
FTPSSAASDA MIQDCIEHGE GLLSSMLSVS GLSRSQVERV IEHVNKGLGE CNRWVHLALV
NSHEKFVLAG PPQSLWAVCL HVRRIRADND LDQSRILFRN RKPIVDILFL PISAPFHTPY
LDGVQDRVIE ALSSASLALH SIKIPLYHTG TGSNLQELQP HQLIPTLIRA ITVDQLDWPL
VCRGLNATHV LDFGPGQTCS LIQELTQGTG VSVIQLTTQS GPKPVGGHLA AVNWEAEFGL
RLHANVHGAA KLHNRMTTLL GKPPVMVAGM TPTTVRWDFV AAVAQAGYHV ELAGGGYHAE
RQFEAEIRRL ATAIPADHGI TCNLLYAKPT TFSWQISVIK DLVRQGVPVE GITIGAGIPS
PEVVQECVQS IGLKHISFKP GSFEAIHQVI QIARTHPNFL IGLQWTAGRG GGHHSWEDFH
GPILATYAQI RSCPNILLVV GSGFGGGPDT FPYLTGQWAQ AFGYPCMPFD GVLLGSRMMV
AREAHTSAQA KRLIIDAQGV GDADWHKSFD EPTGGVVTVN SEFGQPIHVL ATRGVMLWKE
LDNRVFSIKD TSKRLEYLRN HRQEIVSRLN ADFARPWFAV DGHGQNVELE DMTYLEVLRR
LCDLTYVSHQ KRWVDPSYRI LLLDFVHLLR ERFQCAIDNP GEYPLDIIVR VEESLKDKAY
RTLYPEDVSL LMHLFSRRDI KPVPFIPRLD ERFETWFKKD SLWQSEDVEA VIGQDVQRIF
IIQGPMAVQY SISDDESVKD ILHNICNHYV EALQADSRET SIGDVHSITQ KPLSAFPGLK
VTTNRVQGLY KFEKVGAVPE MDVLFEHIVG LSKSWARTCL MSKSVFRDGS RLHNPIRAAL
QLQRGDTIEV LLTADSEIRK IRLISPTGDG GSTSKVVLEI VSNDGQRVFA TLAPNIPLSP
EPSVVFCFKV DQKPNEWTLE EDASGRAERI KALYMSLWNL GFPNKASVLG LNSQFTGEEL
MITTDKIRDF ERVLRQTSPL QLQSWNPQGC VPIDYCVVIA WSALTKPLMV SSLKCDLLDL
LHSAISFHYA PSVKPLRVGD IVKTSSRILA VSVRPRGTML TVSADIQRQG QHVVTVKSDF
FLGGPVLACE TPFELTEEPE MVVHVDSEVR RAILHSRKWL MREDRALDLL GRQLLFRLKS
EKLFRPDGQL ALLQVTGSVF SYSPDGSTTA FGRVYFESES CTGNVVMDFL HRYGAPRAQL
LELQHPGWTG TSTVAVRGPR RSQSYARVSL DHNPIHVCPA FARYAGLSGP IVHGMETSAM
MRRIAEWAIG DADRSRFRSW HITLQAPVHP NDPLRVELQH KAMEDGEMVL KVQAFNERTE
ERVAEADAHV EQETTAYVFC GQGSQRQGMG MDLYVNCPEA KALWARADKH LWEKYGFSIL
HIVQNNPPAL TVHFGSQRGR RIRANYLRMM GQPPIDGRHP PILKGLTRNS TSYTFSYSQG
LLMSTQFAQP ALALMEMAQF EWLKAQGVVQ KGARFAGHSL GEYAALGACA SFLSFEDLIS
LIFYRGLKMQ NALPRDANGH TDYGMLAADP SRIGKGFEEA SLKCLVHIIQ QETGWFVEVV
NYNINSQQYV CAGHFRALWM LGKICDDLSC HPQPETVEGQ ELRAMVWKHV PTVEQVPRED
RMERGRATIP LPGIDIPYHS TMLRGEIEPY REYLSERIKV GDVKPCELVG RWIPNVVGQP
FSVDKSYVQL VHGITGSPRL HSLLQQMA
