ID A0A2T7QFN0_9BACT Unreviewed; 385 AA.
AC A0A2T7QFN0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:PVD54138.1};
GN ORFNames=DC498_01750 {ECO:0000313|EMBL:PVD54138.1};
OS Terrimonas sp.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Terrimonas.
OX NCBI_TaxID=1914338 {ECO:0000313|EMBL:PVD54138.1, ECO:0000313|Proteomes:UP000244333};
RN [1] {ECO:0000313|EMBL:PVD54138.1, ECO:0000313|Proteomes:UP000244333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS-102 {ECO:0000313|EMBL:PVD54138.1,
RC ECO:0000313|Proteomes:UP000244333};
RA Zhang L., Jiang J.;
RT "The draft genome of strain NS-102.";
RL Submitted (APR-2018) 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:PVD54138.1}.
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DR EMBL; QCZJ01000001; PVD54138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7QFN0; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000244333; 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: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; cd08198; DHQS-like; 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:UP000244333}.
FT DOMAIN 81..323
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 385 AA; 43142 MW; DF2EE842E62107E3 CRC64;
MDHIQQRFSV PFEYKVYFTS HLFQQQNTVF ADFLQSDTAG EAKKIFFVID AGVAQTHPSL
VNNIRAYFQE NRQVILIDDI LTVPGGEACK NTDTYVNEII SAVDRYGIDR HSYIAAIGGG
AVLDMAGYAA AIAHRGIRHI RIPTTVLSQN DSGVGVKNGI NYKGKKNFTG TFAPPVAVFN
DAHFLSTLTD RDWRSGIAEA VKVALIKDKP FYIWLTENAQ ALNRREAAPM QYQIKRCAQL
HVDHIADGDP FEKGSSRPLD FGHWSAHKVE QLSGFEIRHG EAVAMGIALD TVYSHLCGWL
SEEDTRQVIQ LLTDLGFDIT HPLMEISGND SPLIKGLHEF REHLGGKLTI MLLKEIGKGE
EVHELDIALL KRSSDWLKQY HQIKQ
//
