W4933_FUSPC
ID W4933_FUSPC Reviewed; 579 AA.
AC K3VAW3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Acyl-CoA ligase FPSE_09184 {ECO:0000303|PubMed:25412204};
DE EC=6.2.1.- {ECO:0000305|PubMed:25412204};
DE AltName: Full=W493 A and B biosynthesis cluster protein FPSE_09184 {ECO:0000303|PubMed:25412204};
GN ORFNames=FPSE_09184;
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096;
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
RN [2]
RP IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=25412204; DOI=10.1021/np500436r;
RA Soerensen J.L., Sondergaard T.E., Covarelli L., Fuertes P.R., Hansen F.T.,
RA Frandsen R.J., Saei W., Lukassen M.B., Wimmer R., Nielsen K.F.,
RA Gardiner D.M., Giese H.;
RT "Identification of the biosynthetic gene clusters for the lipopeptides
RT fusaristatin A and W493 B in Fusarium graminearum and F.
RT pseudograminearum.";
RL J. Nat. Prod. 77:2619-2625(2014).
CC -!- FUNCTION: Acyl-CoA ligase; part of the gene cluster that mediates the
CC biosynthesis of the lipopeptides W493 A and B (PubMed:25412204). W493 A
CC and B consist of six amino acid residues D-allo-thr, L-Ala, D-Ala, L-
CC Gln, D-Tyr, and L-Val/L-Ile linked to a 3-hydroxy-4-methyltetradecanoic
CC acid polyketide chain (PubMed:25412204). The biosynthesis starts with
CC formation of the linear polyketide chain by the highly reducing
CC polyketide synthase PKS40 (PubMed:25412204). The gene cluster contains
CC a putative acyl-CoA ligase (FPSE_09184) for formation of a CoA
CC thioester polyketide. The thiol bond could be hydrolyzed by the
CC putative thioesterase (FPSE_09186) and then accepted by the first T
CC domain in module 1 of NRPS32 (PubMed:25412204). The second T domain is
CC responsible for accepting a threonine, which is adenylated by the A
CC domain and epimerized to the D-allo-threonine formed by the E domain.
CC The five successive modules incorporate Ala, Ala, Gln, Tyr, and Val/Ile
CC into the final product, which is released by cyclization
CC (PubMed:25412204). {ECO:0000269|PubMed:25412204}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:25412204}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AFNW01000306; EKJ70674.1; -; Genomic_DNA.
DR RefSeq; XP_009260576.1; XM_009262301.1.
DR AlphaFoldDB; K3VAW3; -.
DR SMR; K3VAW3; -.
DR STRING; 101028.EKJ70674; -.
DR EnsemblFungi; EKJ70674; EKJ70674; FPSE_09184.
DR GeneID; 20367801; -.
DR KEGG; fpu:FPSE_09184; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; K3VAW3; -.
DR Proteomes; UP000007978; Chromosome 1.
DR Proteomes; UP000007978; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding.
FT CHAIN 1..579
FT /note="Acyl-CoA ligase FPSE_09184"
FT /id="PRO_0000445377"
FT REGION 288..358
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 359..421
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 217..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 358..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 463
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 561
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 579 AA; 63497 MW; 2CDA6DE7E1E39993 CRC64;
MIFTAPAYAP ALPSPLPLQQ TIGDFCLAKR RERQGASDSL FIEAAIDRKW TIDDIEARLG
RMAAALSSAW NITPGQKWHK TVAILASNCV DTLILSWAVH RIGGGCLMLQ PTSSADEMAA
HMDRVPPFAM FLSQDLLTLG QEAFQKSSLS SNVPFYSFSG AEAPKPQQTA VPVASQDAPN
ISTLDDLMAT GKELPLLEKT SFSEGEASRR VAYYCTTSGT SGFQRVVAIT HENIIASILQ
AGLFIEATKG PASEVTLAFL PFNHIYGLLI THTFTWRGDS TVVHSGFNMM EILISIGKHR
INTLYLVPPI INALSRNASI LDRFDMSSVR YIVNGGGPLP KEAFLKMKAA RPDWQIIPGW
GQTEGCGIGS LSSPKDIFPG SSGVLLPGVR IRLRDDDGRI VQGLEEMGEI EIESPSGLFG
YVDYADEALL SPPKEEEFWW PTGDVGLFRI SPNGEQHLFI VDRIRDMIKV KGNQVAPGQI
EDHLTKHAAV AETAVIGIAD EVAGERALAF IVRESSHARE MSEADLRKII QEHNDLELPE
VCRLQDRIIF VDELPKSASG KILKRELRKQ VATWSPPQK
