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Database: UniProt
Entry: F5YHU5_TREPZ
LinkDB: F5YHU5_TREPZ
Original site: F5YHU5_TREPZ 
ID   F5YHU5_TREPZ            Unreviewed;       377 AA.
AC   F5YHU5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:AEF84006.1};
DE            EC=4.2.3.4 {ECO:0000313|EMBL:AEF84006.1};
GN   OrderedLocusNames=TREPR_2362 {ECO:0000313|EMBL:AEF84006.1};
OS   Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84006.1, ECO:0000313|Proteomes:UP000009223};
RN   [1] {ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA   Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA   Paulsen I.T.;
RT   "Complete sequence of Treponema primitia strain ZAS-2.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEF84006.1, ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RX   PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA   Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT   "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT   spirochete species in co-culture.";
RL   ISME J. 5:1133-1142(2011).
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; CP001843; AEF84006.1; -; Genomic_DNA.
DR   RefSeq; WP_015707842.1; NC_015578.1.
DR   AlphaFoldDB; F5YHU5; -.
DR   STRING; 545694.TREPR_2362; -.
DR   KEGG; tpi:TREPR_2362; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_12; -.
DR   OMA; QADSCIG; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000009223; Chromosome.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd08195; DHQS; 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; 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:AEF84006.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT   DOMAIN          63..340
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   377 AA;  39574 MW;  9FEE743800752587 CRC64;
     MLKKNNSFRF GQAVSQVHIR GAIPTLETIL EESGGSPRGV LLVCDTHTEA MAISFAGSDT
     PLCVLESGEA SKTWASVERI IQTAKAAGLG RDGLFIGIGG GVVTDLTSFA ASVYMRGANL
     CLISTTLLGM VDASMGGKTG FDLLGIKNLV GTFFPASHVY LPLDTLATLP PLEWKSGMAE
     LIKTAILDSP ETLEKIKAFR GPFLQRVSGE ANSSGAVIPI LGDLIQQAVL VKGRIVEADP
     RETSAFDGSG SERALLNLGH TFGHALESAA GLGKLSHGEA VAWGMVRSCE LGLALGITPP
     ERAREISEII TAYGYQTEAP HPEIKDTALF MKALGGDKKT KAGIPTFVVP SAERAELVSA
     VSMETGLLKR ILNGEIG
//
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