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Database: UniProt
Entry: U9W2B7_9CYAN
LinkDB: U9W2B7_9CYAN
Original site: U9W2B7_9CYAN 
ID   U9W2B7_9CYAN            Unreviewed;       589 AA.
AC   U9W2B7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:ESA37173.1};
GN   ORFNames=N836_04035 {ECO:0000313|EMBL:ESA37173.1};
OS   Leptolyngbya sp. Heron Island J.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1385935 {ECO:0000313|EMBL:ESA37173.1, ECO:0000313|Proteomes:UP000017515};
RN   [1] {ECO:0000313|EMBL:ESA37173.1, ECO:0000313|Proteomes:UP000017515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Heron Island J {ECO:0000313|EMBL:ESA37173.1,
RC   ECO:0000313|Proteomes:UP000017515};
RX   PubMed=24503993;
RA   Paul R., Jinkerson R.E., Buss K., Steel J., Mohr R., Hess W.R., Chen M.,
RA   Fromme P.;
RT   "Draft Genome Sequence of the Filamentous Cyanobacterium Leptolyngbya sp.
RT   Strain Heron Island J, Exhibiting Chromatic Acclimation.";
RL   Genome Announc. 2:e01166-e01113(2014).
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:ESA37173.1}.
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DR   EMBL; AWNH01000031; ESA37173.1; -; Genomic_DNA.
DR   RefSeq; WP_023072000.1; NZ_AWNH01000031.1.
DR   AlphaFoldDB; U9W2B7; -.
DR   STRING; 1385935.N836_04035; -.
DR   PATRIC; fig|1385935.3.peg.1980; -.
DR   eggNOG; COG0337; Bacteria.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000017515; 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:UP000017515}.
FT   DOMAIN          240..488
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   589 AA;  64840 MW;  B8DA6E6DE27E75D2 CRC64;
     MANTTPAVKA FISTYDNAPF AFQNLDDAIE AVCCGESFRS LILALVNSPA FSEELGKEFE
     AADAIAGLSA CRGLRSCLNF SLGRFFGLLA EVITAFDRAA GNEWTKFSNR VNQSNLGGSK
     LLDRLIRSAD GSFYKDLAAR LVDENPHAVY PTSSYRESEA HVVSAGDDQI IEAVMTSRTF
     TSIRVVENCL DPEQTVLRDM YVSHGRCVCL VDQNVETYYG EQIDKYFKHH GIHLDKLVYR
     AMEVDKGIRT VEKMLGDFKS LGVCRHEPVL IIGGGVIADT GGLACALYHR NTPYVMLSTS
     IVAGIDAGPS PRTCCDGFGY KNLFGAYHAP VLSLTDRFFF KTLREGWLRH GIIEIIKMAA
     IKDLELFEYM EQAGPALIET RFGTLNCEPG SEISVLSQKI LGAALRSYVE AEYGNLYETH
     QCRPHAYGHT WSPGFEIEAG LLHGHAVAIG MGFGAYLSYR KNWITADDFH RILKLISSFG
     LSLWHDVMFN KETLWASQEK IVQKRGGNLA APLPKGGVGK CGYLNSMTQE ELFEAISAYR
     QICNDYPRKG LGIDPLCSDV GLEDPSTIGH SLMETVKAHS GTSEVLSTV
//
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