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Database: UniProt
Entry: E8V1L9_TERSS
LinkDB: E8V1L9_TERSS
Original site: E8V1L9_TERSS 
ID   E8V1L9_TERSS            Unreviewed;       358 AA.
AC   E8V1L9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:ADV82300.1};
DE            EC=4.2.3.4 {ECO:0000313|EMBL:ADV82300.1};
GN   OrderedLocusNames=AciPR4_1477 {ECO:0000313|EMBL:ADV82300.1};
OS   Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV82300.1, ECO:0000313|Proteomes:UP000006844};
RN   [1] {ECO:0000313|EMBL:ADV82300.1, ECO:0000313|Proteomes:UP000006844}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC   {ECO:0000313|Proteomes:UP000006844};
RX   PubMed=23450133; DOI=10.4056/sigs.3036810;
RA   Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA   Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT   "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT   an Acidobacteria from tundra soil.";
RL   Stand. Genomic Sci. 7:59-69(2012).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR   EMBL; CP002467; ADV82300.1; -; Genomic_DNA.
DR   RefSeq; WP_013568033.1; NC_014963.1.
DR   AlphaFoldDB; E8V1L9; -.
DR   STRING; 401053.AciPR4_1477; -.
DR   KEGG; tsa:AciPR4_1477; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_0; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000006844; 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:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
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; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
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   PIRSF; PIRSF001455; DHQ_synth; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ADV82300.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT   DOMAIN          54..315
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   358 AA;  39163 MW;  65B12FAC635C2EB5 CRC64;
     MSASFEIESS TGSYRVEVQR GSFAHSLASF EKSAVVADLF FEPRFKDAGA KAIFVEAIEE
     NKSLDASPAL IERMRASGAN RQTQMVAVGG GIIQDLSAFI ASVYMRGLKW TYMPTTVLAM
     VDSCIGGKSS INVGPYKNLV GTFHPPEVVL IDPDVIETLP EDQRASGLIE AAKICFCRGD
     EAFAKHMAAG PSTSMSADAL EQVIVNSLLS KKWFIEIDEF DKKERLLLNF GHTFGHAIEG
     ATHFGISHGI AVGLGIVCAL EFERGRSVDY SGCARVALLE KHLNEMVRSS PEVAAELKKM
     PMDDVIQRFE SDKKHGTDFY ALILVEPNGD VVLRKVDRSS ETLAAVRRAI ETMIERYA
//
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