ID A0A2N6UY76_9ACTO Unreviewed; 375 AA.
AC A0A2N6UY76;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:PMC89980.1};
GN Name=aroB {ECO:0000313|EMBL:PMC89980.1};
GN ORFNames=CJ184_04415 {ECO:0000313|EMBL:PMC89980.1};
OS Actinotignum urinale.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=190146 {ECO:0000313|EMBL:PMC89980.1};
RN [1] {ECO:0000313|EMBL:PMC89980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0759 {ECO:0000313|EMBL:PMC89980.1};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMC89980.1}.
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DR EMBL; PNHX01000005; PMC89980.1; -; Genomic_DNA.
DR RefSeq; WP_022866482.1; NZ_CP126967.1.
DR AlphaFoldDB; A0A2N6UY76; -.
DR STRING; 1120933.GCA_000420445_01000; -.
DR OrthoDB; 9806583at2; -.
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 71..334
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 375 AA; 40919 MW; D40670828E2283DB CRC64;
MTTQRIDIQL TRTIDESYPL IIGRNLTDSL KDVLAEPRYA KRKVAVITDS TVADLVARAV
AEDLGERAQL FVFPAGEKSK VRATKERLED AMLDAGFNRD SVIVAIGGGV VSDLAGFVAA
TFTRGIPYIT WTTTLVGAAD AAIGGKTAVD THHATNLIGA FHQPGAVLID VERWLTLDDS
QIRDGMGETV KHACLADAHY FDVLENAFVE RKMGLHECVA DEELSQYIAE RNARIKQDFV
QSDVHEGNRR MGLNLGHTIG RALEAAMGFT MTHGECVAVG LLLQAKLGLH FGYVSEGDVA
RMERLLKAIG LPTEIPENVT VDAIMDAMEH DKKALGGKTR FVFQHGIGAL EVFEGGAYAR
EIDADIIREF LEAQR
//
