ID A0A1E4L5X3_9PROT Unreviewed; 363 AA.
AC A0A1E4L5X3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=3-dehydroquinate synthase domain-containing protein {ECO:0000259|Pfam:PF01761};
GN ORFNames=ABS92_03505 {ECO:0000313|EMBL:ODU50281.1};
OS Thiobacillus sp. SCN 63-374.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660149 {ECO:0000313|EMBL:ODU50281.1, ECO:0000313|Proteomes:UP000094238};
RN [1] {ECO:0000313|EMBL:ODU50281.1, ECO:0000313|Proteomes:UP000094238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU50281.1}.
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DR EMBL; MEFK01000028; ODU50281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4L5X3; -.
DR Proteomes; UP000094238; Unassembled WGS sequence.
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: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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 53..315
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 363 AA; 39226 MW; C042BC3B2B0ACDDF CRC64;
MSVSFDINSE IKPYQVEIGE GLLEATLKAA GDSIFLCDSF FAGRLAPCGR PIIAIDATEY
AKSLDRMSEV IIRLRDSGAT RSTNLIAVGG GVIQDVATFC ASIYMRGISW KYLPTTLLGM
VDSCIGGKSA INVGPYKNIV GNFYPPDEIL VDPDLCGTLA VEQKVAGLCE AAKICYARGG
DAFARYLVLH PSAELKNINL SHLIELSLRS KKWFIEVDEF DRNERLLLNF GHTFGHAIEG
AAQFAVSHGV AVGVGILAAI HYARISTGKE TLPQSTATLA THIRGLLAHI DGLGGVLATT
TEQDLFDRFA ADKKHTSTAY TIVGIDKAGR LQRLALPRSS ESENMIRETF KAIRQPDFLS
AAE
//
