ID   A0A429RX80_9ACTN        Unreviewed;       466 AA.
AC   A0A429RX80;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:RSS78588.1};
GN   ORFNames=EF918_20445 {ECO:0000313|EMBL:RSS78588.1};
OS   Streptomyces sp. WAC06614.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS78588.1, ECO:0000313|Proteomes:UP000277644};
RN   [1] {ECO:0000313|EMBL:RSS78588.1, ECO:0000313|Proteomes:UP000277644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC06614 {ECO:0000313|EMBL:RSS78588.1,
RC   ECO:0000313|Proteomes:UP000277644};
RA   Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT   "Unmasking the antibiotic production potential of Actinomycetes through
RT   CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RSS78588.1}.
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DR   EMBL; RPRY01000149; RSS78588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429RX80; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000277644; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd08197; DOIS; 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   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}; Membrane {ECO:0000256|SAM:Phobius};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000277644};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        190..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          163..417
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  50068 MW;  FC500DB97B6CA35A CRC64;
     MLRRCPRRAR RRGRCGPNSR SPARSPQFPS ARAACQVVRP PGFVSATLPR VGNLWQVNEG
     EVAKRCQALV RSRPTSEPVN GEVVTLLAEK TTVTEREVRF GDVRYGFSVG HGPESLGALT
     RKLEGLDADR FVIVADTGLT QDQIDEIARC AGEVAPTTVL TAVADEKAKS LDVVSALAER
     LIPTGITRRS VVIALGGGLV GNMAGLLSAL VFRGIRLVHV PTTLLAMSDS VLSLKQAVNT
     SVGKNHLGTF YAPVFVWNHL DFLRTLPADE IRSALCEMIK NVLGIVPDRY DEVAARLRPD
     ARYTPEDFAW FIDLCVEAKC AVMRDDKTER GDALILEYGH TIGHAAELLT GGELRHGYAI
     GLGMLAVARI ARELGLLTAE DEAAHRTLLT LNGAPTVLPA GVTVDAVLRT IALDNKRGYV
     KATAGTRDLI LLEGLGKPHR PGGAQITQVP EAIVRLGVES IAGEVA
//