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Database: UniProt
Entry: A0A367L4C8_9HYPO
LinkDB: A0A367L4C8_9HYPO
Original site: A0A367L4C8_9HYPO 
ID   A0A367L4C8_9HYPO        Unreviewed;       443 AA.
AC   A0A367L4C8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=3-dehydroquinate synthase domain-containing protein {ECO:0000259|Pfam:PF01761};
GN   ORFNames=L249_1470 {ECO:0000313|EMBL:RCI09286.1};
OS   Ophiocordyceps polyrhachis-furcata BCC 54312.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=1330021 {ECO:0000313|EMBL:RCI09286.1, ECO:0000313|Proteomes:UP000253664};
RN   [1] {ECO:0000313|EMBL:RCI09286.1, ECO:0000313|Proteomes:UP000253664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 54312 {ECO:0000313|EMBL:RCI09286.1,
RC   ECO:0000313|Proteomes:UP000253664};
RX   PubMed=26511477; DOI=10.1186/s12864-015-2101-4;
RA   Wichadakul D., Kobmoo N., Ingsriswang S., Tangphatsornruang S.,
RA   Chantasingh D., Luangsa-ard J.J., Eurwilaichitr L.;
RT   "Insights from the genome of Ophiocordyceps polyrhachis-furcata to
RT   pathogenicity and host specificity in insect fungi.";
RL   BMC Genomics 16:881-881(2015).
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RCI09286.1}.
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DR   EMBL; LKCN02000016; RCI09286.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367L4C8; -.
DR   STRING; 1330021.A0A367L4C8; -.
DR   Proteomes; UP000253664; 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:UP000253664}.
FT   DOMAIN          85..331
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   443 AA;  48630 MW;  EA0B4971762D4A7B CRC64;
     MSDMKATVEQ TSNGFSVRGY EKIEYDFEFL DGVFEARNSQ LADCYRPWGR CLAVMDLNIY
     VLYGHLMRRY FEAHDIALSV HKTAIGEKAK SVETLLSIVD SMDRFGVVRK EPVLVGRGGL
     VTDVAGFACA AYRRTTNYIR IPTTVIGLID AAVSIKVAVN YGRCKNRLGA YHAPIHTFLD
     FTFLRTLPTA QIRNGFAELI KISSCADADT FDLLDAHCEH LICSAFARAD GSDSGLKEVA
     DRICRAGIYE MLRLETPNLH ELMLDRVIAY GHTWSPIFEL VPEPHLRHGH AISIDMAYSA
     TLAHRRGLLS GPEHRRLLRL FSRAGLAMDH AGFDAAILDR ATAAILKTRD GLLRAPVPVS
     PIGRCVFLND VSGEEMRAAL EEHKRLVASF PRRGEGVDAF VDASDTGYTA VQQPADVVVT
     TLGKTGRAAA EVSVSAVVTN GVA
//
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