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Database: UniProt
Entry: W0ETR0_9BACT
LinkDB: W0ETR0_9BACT
Original site: W0ETR0_9BACT 
ID   W0ETR0_9BACT            Unreviewed;       341 AA.
AC   W0ETR0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:AHF14170.1};
GN   ORFNames=NIASO_01130 {ECO:0000313|EMBL:AHF14170.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF14170.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF14170.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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; CP007035; AHF14170.1; -; Genomic_DNA.
DR   RefSeq; WP_008582155.1; NZ_CP007035.1.
DR   AlphaFoldDB; W0ETR0; -.
DR   STRING; 929713.NIASO_01130; -.
DR   KEGG; nso:NIASO_01130; -.
DR   eggNOG; COG0337; Bacteria.
DR   HOGENOM; CLU_001201_0_1_10; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000003586; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide 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; IPR016037; DHQ_synth_AroB.
DR   InterPro; IPR030963; DHQ_synth_fam.
DR   InterPro; IPR030960; DHQS/DOIS.
DR   NCBIfam; TIGR01357; aroB; 1.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003586};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          54..305
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   341 AA;  38176 MW;  193894FEB0F783A9 CRC64;
     MEKIIKFSTA ATHFYFAAAI SKLKEIADKK MAVIITDEHI YTAHSKKFSG WKTIVLKPGE
     QYKVQPTVDE VIQQLIGLQA DRKTTLIGVG GGVITDITGY IASVYMRGLR FGFVPTSILG
     LVDASIGGKN GIDVGPYKNM VGVIRQPSFI LHDMNLLNSL PQLEWENGFA EVIKHACIKD
     AALFAALEKN TLKDYQSRRK TIAELVERNA LIKIRVVQKD EFEKGDRRLL NLGHTLGHAI
     ETQYNLIHGH AIAIGMVAAC RISEQLSGFK QTERVVQLLE RYHLPTHLDF DPGKVFEVLK
     MDKKRELKTM NFVLLDKIGK AVVRAIPMKQ LEQIIGGLNQ K
//
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