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Database: UniProt
Entry: G8QWN7_SPHPG
LinkDB: G8QWN7_SPHPG
Original site: G8QWN7_SPHPG 
ID   G8QWN7_SPHPG            Unreviewed;       353 AA.
AC   G8QWN7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=3-dehydroquinate synthetase {ECO:0000313|EMBL:AEV28331.1};
GN   OrderedLocusNames=SpiGrapes_0476 {ECO:0000313|EMBL:AEV28331.1};
OS   Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC   Sphaerochaeta.
OX   NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV28331.1, ECO:0000313|Proteomes:UP000005632};
RN   [1] {ECO:0000313|EMBL:AEV28331.1, ECO:0000313|Proteomes:UP000005632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes
RC   {ECO:0000313|Proteomes:UP000005632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Ritalahtilisa K.,
RA   Loeffler F., Woyke T.;
RT   "Complete sequence of Spirochaeta sp. grapes.";
RL   Submitted (NOV-2011) 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; CP003155; AEV28331.1; -; Genomic_DNA.
DR   RefSeq; WP_014269180.1; NC_016633.1.
DR   AlphaFoldDB; G8QWN7; -.
DR   STRING; 158190.SpiGrapes_0476; -.
DR   KEGG; sgp:SpiGrapes_0476; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_12; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000005632; Chromosome.
DR   GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005632}.
FT   DOMAIN          57..317
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   353 AA;  38838 MW;  A76F03109B2B976C CRC64;
     MKSLSTTTLA NGKQTEILIA DNLKDLSAHL GSYGRSVLWV FDANTATLFK QLPPVNVVLE
     SGESSKNFSS LERILSNAVD EGLARDCRII GFGGGVVCDM AAFAASVFMR GCKLTLVPTT
     LLCMVDASVG GKTAIDFKGL KNMVGSFYPA EEVLISMDTL RTLPEKEYLN GLAEVIKHAL
     LSQDEQLYKF LLVKKNEILS RDIETLQTLV TLSLAVKQWY IEQDPTETKG IRQVLNLGHT
     FGHALESSGH FTFGHGACVA WGTCRALEAG VNMGITDKAY AIGATKLFKS YGYDIDYRIG
     RGDWIEFRER LSKDKKKEKG QVLFVLMESQ GKAVLRPIDM ALVQHLVIAK PIF
//
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