ID K9YA00_HALP7 Unreviewed; 587 AA.
AC K9YA00;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:AFZ43776.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:AFZ43776.1};
GN OrderedLocusNames=PCC7418_1590 {ECO:0000313|EMBL:AFZ43776.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ43776.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003945; AFZ43776.1; -; Genomic_DNA.
DR RefSeq; WP_015225652.1; NC_019779.1.
DR AlphaFoldDB; K9YA00; -.
DR SMR; K9YA00; -.
DR STRING; 65093.PCC7418_1590; -.
DR KEGG; hao:PCC7418_1590; -.
DR PATRIC; fig|65093.3.peg.1693; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_465996_0_0_3; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000010481; Chromosome.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:AFZ43776.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000010481}.
FT DOMAIN 240..492
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT REGION 568..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 65388 MW; 5A87E1C954389FF4 CRC64;
MTKTTSAVKA FIATYNNEPL TKEDLNEAVE AIIGTTPFRH LLLSLIDSDA FSPDLGEEFA
EAEAIEGLAA CRQLRTCLNH SLSHFFGLLA QLIAGFDENA ASEWYRFSNR IHHSEIAKTK
LLDCLLQSED GKFYQELSSR LVETDPHAVY PTSSYRQSRG YVVSTEDDQT VEAVMSASTF
TSIKVLENCL DPQETVLRDL YISLGRCVCL VDQNVEQYYG EQINNYFEYH EIQLDKLVYR
AMEVDKGIHT VERMLGDFKR LGVSRNEPVL IVGGGVLTDT GGLACALYHR NTPYVMLSTS
IVAGIDAGPS PRTCCDGFGY KNLFGAYHAP ILSLTDRSFF KTLREGWLRH GIAEILKMAA
VKDAELFSDL EEAGEDLITT RFGTLNSEQN DKISVLSQKI LGAAMRSYVE AEYDNLYETH
QCRPHAYGHT WSPGFEIEAG LLHGHAVAVG MGFSAYLSYR NNWLSHEDFH RILKLISSFG
LSLWHDVLLN EETVWAAQEK MVQKRGGNLA APMPKGEIGK CGYLNQLSRE ELGSAIAQYQ
AICAEYPRKG LGIEAHCHEV GLENPSTVGH HLPVNTSEEP EELLSTV
//
