ID   A0A319CA02_9EURO        Unreviewed;       474 AA.
AC   A0A319CA02;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Putative 3-dehydroquinate synthase {ECO:0000313|EMBL:PYH81040.1};
GN   ORFNames=BO82DRAFT_311813 {ECO:0000313|EMBL:PYH81040.1};
OS   Aspergillus uvarum CBS 121591.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH81040.1, ECO:0000313|Proteomes:UP000248340};
RN   [1] {ECO:0000313|EMBL:PYH81040.1, ECO:0000313|Proteomes:UP000248340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH81040.1,
RC   ECO:0000313|Proteomes:UP000248340};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; KZ821705; PYH81040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319CA02; -.
DR   STRING; 1448315.A0A319CA02; -.
DR   VEuPathDB; FungiDB:BO82DRAFT_311813; -.
DR   OrthoDB; 453at2759; -.
DR   Proteomes; UP000248340; 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:UP000248340}.
FT   DOMAIN          85..333
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   474 AA;  52952 MW;  67E10B6C52460F34 CRC64;
     MSDLKATVSE TKNGFHVEGY EKIEYDFTFL DGVFDPQNAQ LAGLYERWGR CLAIMDKNIY
     DLYGEQMQKY FDHHGLELKI HQTMIGEKAK SLETFTEIVD SMTGFGIIRK EPVLVVGGGL
     VTDVAGFACA AYRRNTNYIR IPTTVIGLID ASVSIKVAVN YGNYKNRLGA YHAPMHTFLD
     FGFLRTLPEA QVRNGFAELI KISSCAHLRT FDLLDEFCER LIATKFGRSQ DETGEVRKAA
     DEINRNGIFE MLKLESPNLH EIGLDRVIAY GHTWSPLHEL APPVPLRHGH AISIDMAYSA
     TLANIRGLLS DAEHRRLLNL FSRAGLSMDH ELFNEEILDK ATQAILKTRD GLLRAAVPCP
     LGSCKFLNDV TNEEMFAALR RHKELMKEYP RQGAGIEAYV DASDTGYTIN NQPVDPQIHA
     QQKMVDGGEK KTNGVAEGKK LNGVVDEKKN VFSDGVMNGF RQIAANGYPN GLRN
//