ID A0A2V1DZ15_9PLEO Unreviewed; 454 AA.
AC A0A2V1DZ15;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=2-epi-5-epi-valiolone synthase-like protein {ECO:0000313|EMBL:PVI02614.1};
GN ORFNames=DM02DRAFT_559554 {ECO:0000313|EMBL:PVI02614.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI02614.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI02614.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI02614.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR EMBL; KZ805341; PVI02614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1DZ15; -.
DR STRING; 97972.A0A2V1DZ15; -.
DR Proteomes; UP000244855; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd08199; EEVS; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR030960; DHQS/DOIS.
DR InterPro; IPR035872; EEVS-like.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF1; 3-DEHYDROQUINATE SYNTHASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000244855}.
FT DOMAIN 86..336
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT REGION 423..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 50805 MW; 3A0BC6831649A2E5 CRC64;
MSDLKASVHE TKNGFHVEGY EKIEYDFTFL DGVFNLENAQ LAKCYEQWGR TLAVMDLNIY
NLYGEKMQKY FDHYGLELRI HKTMIGEKAK SMDTLLRIVD SMTDFGIIRK EPVLVVGGGL
VTDVAGFACA AYRRNTNFIR IPTTVIGLID ASVSIKVAVN YGNYKNRLGA YHAPIHTFLD
FGFLRTLPEG QVRNGFAELI KISSCAHLPT FDLLDKYCEK LIETRFGRSD DATQEIRQAA
DEINRAGIYE MLKLETPNLH EIGLDRVIAY GHTWSPLHEL SPSVPLRHGH AISIDMAYSA
TLANHRGLLS EEEHQRILKL FSRAGLSMDH ELFDEEMLDK ATKAILKTRD GKLRAAVPNP
LGNCTFLNDV APAEMNEALR KHKQIMKQYP RNGEGIDAFV DASDTGYTVN DTPVEEVTAN
GKMANGKTSG HTHGNSVPDA LRQAVNGYPN GYKN
//
