AFLA_ASPPU
ID AFLA_ASPPU Reviewed; 1671 AA.
AC Q8TGA2; A0A0F0HZ47;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Fatty acid synthase alpha subunit aflA {ECO:0000303|PubMed:16256699};
DE EC=2.3.1.86 {ECO:0000305|PubMed:16256699};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000305|PubMed:16256699};
DE EC=1.1.1.100 {ECO:0000305|PubMed:16256699};
DE AltName: Full=Beta-ketoacyl reductase {ECO:0000305};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000305|PubMed:16256699};
DE EC=2.3.1.41 {ECO:0000305|PubMed:16256699};
DE AltName: Full=Aflatoxin biosynthesis protein A {ECO:0000303|PubMed:15006741};
GN Name=aflA {ECO:0000303|PubMed:15006741};
GN Synonyms=fas-2 {ECO:0000303|PubMed:15094053}, fas-2A,
GN hexA {ECO:0000303|PubMed:16256699}; ORFNames=P875_00052994;
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.
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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).
CC -!- FUNCTION: Fatty acid synthase alpha 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,
CC PubMed:15094053). The four major aflatoxins produced by A.parasiticus
CC are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and
CC aflatoxin G2 (AFG2) (PubMed:15006741). 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). AflC combines a hexanoyl starter unit and 7 malonyl-
CC CoA extender units to synthesize the precursor NOR (PubMed:18403714).
CC The hexanoyl starter unit is provided to the acyl-carrier protein (ACP)
CC domain by the fungal fatty acid synthase aflA/aflB (PubMed:16256699).
CC The second step is the conversion of NOR to averantin (AVN) and
CC requires the norsolorinic acid ketoreductase aflD, which catalyzes the
CC dehydration of norsolorinic acid to form (1'S)-averantin
CC (PubMed:10584035). The norsolorinic acid reductases aflE and aflF may
CC also play a role in the conversion of NOR to AVN (PubMed:15006741). The
CC cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of
CC AVN to 5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is
CC performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms
CC HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin
CC (AVF) by aflK that plays a dual role in the pathway, as a 5'-
CC oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as
CC well as a versicolorin B synthase in a later step in the pathway
CC (PubMed:15006741, PubMed:11055914, PubMed:15932995). The averufin
CC oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal
CC acetate (VHA) (PubMed:15006741). VHA is then the substrate for the
CC versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL)
CC (PubMed:15006741). Versicolorin B synthase aflK then converts VAL to
CC versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which
CC is required for DNA-binding, thus giving to aflatoxin its activity as a
CC mutagen (PubMed:15006741, PubMed:8368837, PubMed:15932995). Then, the
CC activity of the versicolorin B desaturase aflL leads to versicolorin A
CC (VERA) (PubMed:15006741, PubMed:8368837). A branch point starts from
CC VERB since it can also be converted to dihydrodemethylsterigmatocystin
CC (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins
CC B1 and G1, and DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next,
CC the versicolorin reductase aflM and the cytochrome P450 monooxygenase
CC aflN are involved in conversion of VERA to demethylsterigmatocystin
CC (DMST) (PubMed:15006741, PubMed:1339261, PubMed:15771506). AflX and
CC aflY seem also involved in this step, through probable aflX-mediated
CC epoxide ring-opening step following versicolorin A oxidation and aflY-
CC mediated Baeyer-Villiger oxidation required for the formation of the
CC xanthone ring (PubMed:16332900, PubMed:16461654). The methyltransferase
CC aflO then leads to the modification of DMST to sterigmatocystin (ST),
CC and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813). Both
CC ST and DHST are then substrates of the O-methyltransferase aflP to
CC yield O-methylsterigmatocystin (OMST) and dihydro-O-
CC methylsterigmatocystin (DHOMST), respectively (PubMed:8434913). Finally
CC OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2
CC and G2, via the action of several enzymes including O-
CC methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450
CC monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase
CC nadA which is specifically required for the synthesis of AFG1
CC (PubMed:15006741, PubMed:11996570, PubMed:15528514, PubMed:18486503).
CC {ECO:0000269|PubMed:10543813, ECO:0000269|PubMed:10584035,
CC ECO:0000269|PubMed:11055914, ECO:0000269|PubMed:11996570,
CC ECO:0000269|PubMed:1339261, ECO:0000269|PubMed:15528514,
CC ECO:0000269|PubMed:15771506, ECO:0000269|PubMed:15932995,
CC ECO:0000269|PubMed:16256699, ECO:0000269|PubMed:16332900,
CC ECO:0000269|PubMed:16461654, ECO:0000269|PubMed:18403714,
CC ECO:0000269|PubMed:18486503, ECO:0000269|PubMed:8368836,
CC ECO:0000269|PubMed:8368837, ECO:0000269|PubMed:8434913,
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=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000255|PROSITE-ProRule:PRU10022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
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 -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of the acyl carrier domain by the C-terminal PPT domain. This
CC modification is essential for activity because fatty acids are bound in
CC thioester linkage to the sulfhydryl of the prosthetic group.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KJK60794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF391094; AAL99898.1; -; Genomic_DNA.
DR EMBL; AY371490; AAS66002.1; -; Genomic_DNA.
DR EMBL; JZEE01000728; KJK60794.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q8TGA2; -.
DR SMR; Q8TGA2; -.
DR STRING; 1403190.Q8TGA2; -.
DR PRIDE; Q8TGA2; -.
DR EnsemblFungi; KJK60794; KJK60794; P875_00052994.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; TAS:GO_Central.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..1671
FT /note="Fatty acid synthase alpha subunit aflA"
FT /id="PRO_0000438336"
FT DOMAIN 75..153
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000305|PubMed:16256699"
FT REGION 40..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..729
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16256699"
FT REGION 833..1417
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:16256699"
FT REGION 1244..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1113
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 1552..1554
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1552
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1598..1608
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1622..1625
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1652..1654
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1653
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT MOD_RES 113
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1671 AA; 181275 MW; 266034C51A556FFE CRC64;
MVIQGKRLAA SSIQLLASSL DAKKLCYEYD ERQAPGVTQI TEEAPTEQPP LSTPPSLPQT
PNISPISASK IVIDDVALSR VQIVQALVAR KLKTAIAQLP TSKSIKELSG GRSSLQNELV
GDIHNEFSSI PDAPEQILLR DFGDANPTVQ LGKTSSAAVA KLISSKMPSD FNANAIRAHL
ANKWGLGPLR QTAVLLYAIA SEPPSRLASS SAAEEYWDNV SSMYAESCGI TLRPRQDTMN
EDAMASSAID PAVVAEFSKG HRRLGVQQFQ ALAEYLQIDL SGSQASQSDA LVAELQQKVD
LWTAEMTPEF LAGISPMLDV KKSRRYGSWW NMARQDVLAF YRRPSYSEFV DDALAFKVFL
NRLCNRADEA LLNMVRSLSC DAYFKQGSLP GYHAASRLLE QAITSTVADC PKARLILPAV
GPHTTITKDG TIEYAEAPRQ GVSGPTAYIQ SLRQGASFIG LKSADVDTQS NLTDALLDAM
CLALHNGISF VGKTFLVTGA GQGSIGAGVV RLLLEGGARV LVTTSREPAT TSRYFQQMYD
NHGAKFSELR VVPCNLASAQ DCEGLIRHVY DPRGLNWDLD AILPFAAASD YSTEMHDIRG
QSELGHRLML VNVFRVLGHI VHCKRDAGVD CHPTQVLLPL SPNHGIFGGD GMYPESKLAL
ESLFHRIRSE SWSDQLSICG VRIGWTRSTG LMTAHDIIAE TVEEHGIRTF SVAEMALNIA
MLLTPDFVAH CEDGPLDADF TGSLGTLGSI PGFLAQLHQK VQLAAEVIRA VQAEDEHERF
LSPGTKPTLQ APVAPMHPRS SLRVGYPRLP DYEQEIRPLS PRLERLQDPA NAVVVVGYSE
LGPWGSARLR WEIESQGQWT SAGYVELAWL MNLIRHVNDE SYVGWVDTQT GKPVRDGEIQ
ALYGDHIDNH TGIRPIQSTS YNPERMEVLQ EVAVEEDLPE FEVSQLTADA MRLRHGANVS
IRPSGNPDAC HVKLKRGAVI LVPKTVPFVW GSCAGELPKG WTPAKYGIPE NLIHQVDPVT
LYTICCVAEA FYSAGITHPL EVFRHIHLSE LGNFIGSSMG GPTKTRQLYR DVYFDHEIPS
DVLQDTYLNT PAAWVNMLLL GCTGPIKTPV GACATGVESI DSGYESIMAG KTKMCLVGGY
DDLQEEASYG FAQLKATVNV EEEIACGRQP SEMSRPMAES RAGFVEAHGC GVQLLCRGDI
ALQMGLPIYA VIASSAMAAD KIGSSVPAPG QGILSFSRER ARSSMISVTS RPSSRSSTSS
EVSDKSSLTS ITSISNPAPR AQRARSTTDM APLRAALATW GLTIDDLDVA SLHGTSTRGN
DLNEPEVIET QMRHLGRTPG RPLWAICQKS VTGHPKAPAA AWMLNGCLQV LDSGLVPGNR
NLDTLDEALR SASHLCFPTR TVQLREVKAF LLTSFGFGQK GGQVVGVAPK YFFATLPRPE
VEGYYRKVRV RTEAGDRAYA AAVMSQAVVK IQTQNPYDEP DAPRIFLDPL ARISQDPSTG
QYRFRSDATP ALDDDALPPP GEPTELVKGI SSAWIEEKVR PHMSPGGTVG VDLVPLASFD
AYKNAIFVER NYTVRERDWA EKSADVRAAY ASRWCAKEAV FKCLQTHSQG AGAAMKEIEI
EHGGNGAPKV KLRGAAQTAA RQRGLEGVQL SISYGDDAVI AVALGLMSGA S
