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
//