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
//