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Database: UniProt
Entry: K9UHE7_CHAP6
LinkDB: K9UHE7_CHAP6
Original site: K9UHE7_CHAP6 
ID   K9UHE7_CHAP6            Unreviewed;       413 AA.
AC   K9UHE7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=3-dehydroquinate synthetase {ECO:0000313|EMBL:AFY93856.1};
GN   ORFNames=Cha6605_2820 {ECO:0000313|EMBL:AFY93856.1};
OS   Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC   Chamaesiphon.
OX   NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY93856.1, ECO:0000313|Proteomes:UP000010366};
RN   [1] {ECO:0000313|EMBL:AFY93856.1, ECO:0000313|Proteomes:UP000010366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL   Submitted (MAY-2012) 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; CP003600; AFY93856.1; -; Genomic_DNA.
DR   RefSeq; WP_015160001.1; NC_019697.1.
DR   AlphaFoldDB; K9UHE7; -.
DR   STRING; 1173020.Cha6605_2820; -.
DR   KEGG; cmp:Cha6605_2820; -.
DR   PATRIC; fig|1173020.3.peg.3218; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_4_3; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000010366; Chromosome.
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:UP000010366}.
FT   DOMAIN          83..338
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   413 AA;  45646 MW;  6E6A5613408D12E7 CRC64;
     MTNVQATFKA TETAFHVEGY EKIDFSLLYV DGAFAVENAE IAESYRQFGR CLMVVDEAVY
     GLYAEQIQAY FQHYQIDLTV FPVAIKETDK TLQSVEKIVD AFADFGLVRK EPVLVVGGGL
     TTDVAGFACA TYRRRTNYIR VPTTLIGLID ASVAIKVAVN HGKLKNRLGA YHASQKVILD
     FSFLKTLPVD QVRNGMAELI KIAVVANNGI FEMLEKYGED LLHTHFGYLN GTPELREVAH
     KVTYDAINTM LGLEVPNLHE LDLDRVIAYG HTWSPTLELT PAIPMFHGHG VNIDMAFSAT
     IAQERGYISV GERNRILGLM SRIGLAIDSS YLTPELLWKA TESIGRTRDG LLRAAVPHPI
     GSCSFLNDLT RAELDEHLAI HKEICREYPR GGDGEDMFMS LASVAPASVG VEA
//
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