ID I3ZFB6_TERRK Unreviewed; 358 AA.
AC I3ZFB6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=3-dehydroquinate synthetase {ECO:0000313|EMBL:AFL87934.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:AFL87934.1};
GN OrderedLocusNames=Terro_1630 {ECO:0000313|EMBL:AFL87934.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL87934.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL87934.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003379; AFL87934.1; -; Genomic_DNA.
DR RefSeq; WP_014785503.1; NC_018014.1.
DR AlphaFoldDB; I3ZFB6; -.
DR STRING; 926566.Terro_1630; -.
DR KEGG; trs:Terro_1630; -.
DR PATRIC; fig|926566.3.peg.1612; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_1_0; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000006056; 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:AFL87934.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006056}.
FT DOMAIN 54..315
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 358 AA; 38558 MW; A9F346ABB93574E9 CRC64;
MSASFDIQSA TGTYNVTVES GSFAQTLAGM QDAAVIADAF FKPALAGIGI DAIFVEAIES
NKSLDASPAL IEQMRKAGAN RSTHMVAVGG GIIQDLSAFI ASVYMRGLRW TYMPTTVLAM
VDSCIGGKSS INVGPYKNLV GTFHSPERVW IDPAVIATLP ADQRASGLIE AAKITFCRGA
EAFEEHLACG PSVDMDPAAL ERLIINSLHS KKWFIEIDEF DRKERLLLNF GHTFGHAIEG
ASHFGIAHGI AVGIGIECAI AFQENAGVDY TAVPRVAALR QHLRDMIGND PTVLGHLREL
SVDDVLQRFV SDKKHGKDFY ALILIAPDGS VILSREPRTE ATLGSVRRAV EEIIEAYV
//
