DTXS4_METRA
ID DTXS4_METRA Reviewed; 501 AA.
AC E9FCP7;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 2.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=L-aspartate decarboxylase dtxS4 {ECO:0000305};
DE EC=4.1.1.11 {ECO:0000305|PubMed:22232661};
DE AltName: Full=Destruxin synthesis protein 4 {ECO:0000303|PubMed:22232661};
GN Name=dtxS4 {ECO:0000303|PubMed:22232661}; ORFNames=MAA_10046;
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075;
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22232661; DOI=10.1073/pnas.1115983109;
RA Wang B., Kang Q., Lu Y., Bai L., Wang C.;
RT "Unveiling the biosynthetic puzzle of destruxins in Metarhizium species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:1287-1292(2012).
CC -!- FUNCTION: L-aspartate decarboxylase; part of the gene cluster that
CC mediates the biosynthesis of destruxins, insecticidal cyclic
CC hexadepsipeptides which induce flaccid paralysis and visceral muscle
CC contraction in insects through targeting the calcium channels and
CC vacuolar-type ATPases (PubMed:22232661). The aldo-keto reductase dtxS3
CC converts alpha-ketoisocaproic acid from deaminated leucine into alpha-
CC hydroxyisocaproic acid (HIC), which is the first substrate for
CC destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate
CC decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last
CC substrate for the destruxin assembly line performed by dtxS1
CC (PubMed:22232661). The nonribosomal peptide synthetase dtxS1
CC synthesizes destruxins B and B2, whereas the cytochrome P450
CC monooxygenase dtxS2 is required to convert destruxin B into other
CC destruxin derivatives, including destructins C, D, A and E
CC (PubMed:22232661). Destruxin E-diol (ED) is further produced in a non-
CC enzymatic manner from destruxin E (PubMed:22232661). Destruxins play an
CC important role in virulence and escape from insect host immune defenses
CC (PubMed:22232661). {ECO:0000269|PubMed:22232661}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:57966; EC=4.1.1.11;
CC Evidence={ECO:0000305|PubMed:22232661};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q99259};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:22232661}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of destruxins
CC (PubMed:22232661). {ECO:0000269|PubMed:22232661}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; ADNJ02000010; EFY94503.2; -; Genomic_DNA.
DR RefSeq; XP_007826235.2; XM_007828044.2.
DR AlphaFoldDB; E9FCP7; -.
DR SMR; E9FCP7; -.
DR EnsemblFungi; EFY94503; EFY94503; MAA_10046.
DR GeneID; 19264332; -.
DR KEGG; maj:MAA_10046; -.
DR HOGENOM; CLU_011856_0_0_1; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..501
FT /note="L-aspartate decarboxylase dtxS4"
FT /id="PRO_0000436439"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT BINDING 474
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
FT MOD_RES 320
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q99259"
SQ SEQUENCE 501 AA; 55020 MW; D36D3CE1A8F03AA7 CRC64;
MRDTKKMLNR ADELDDLYEA VRALIIPHVR AADEACSLKS AGQLHTDDTQ RLQNVLVEPY
PPKALQERFQ FTLPDNEGNG KDGLMHLIRD VLRYSVNTWD QGFMDKLTSS TNPVGVISEI
VLGILNTNVH VYHVAPALSV IEKVTGRTLA AYFGFNSPSA GGISCQGGSA SNLTSLVVAR
NSLYPDCKLN GGSSYQFAIF TSCHGHFSME KAAITCGMGL SSVVHVPVND DGRMNVSALR
ELVIQAKAQG KTPLYVNATA GTTVLGVFDP LHEIKTICEE FGMWFHVDAS WGGSIIFSAK
HRHKLTGCEL ADSLTISPHK MLNVPMTCSF LLTNNLSSFY TANSLDAGYL FHDTEDDEVW
DLANLTLQCG RRADSLKMAL AWTYYGAAGF ERRINHAFKM AAHLSSIIQK SPDFELVSPN
PPPCLQVCFY YTPGGKMAKS EMETSRRTRA MVEKMVDRGF MFDFAPGPKG DFFRVVVNCE
TLLGTVEGLF KGLEAVGKQV V
