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Database: UniProt
Entry: A0A2N1F842_9FLAO
LinkDB: A0A2N1F842_9FLAO
Original site: A0A2N1F842_9FLAO 
ID   A0A2N1F842_9FLAO        Unreviewed;       352 AA.
AC   A0A2N1F842;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:PKH51079.1};
GN   Name=aroB {ECO:0000313|EMBL:PKH51079.1};
GN   ORFNames=CXF68_10455 {ECO:0000313|EMBL:PKH51079.1};
OS   Tenacibaculum sp. Bg11-29.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=2058306 {ECO:0000313|EMBL:PKH51079.1, ECO:0000313|Proteomes:UP000233844};
RN   [1] {ECO:0000313|EMBL:PKH51079.1, ECO:0000313|Proteomes:UP000233844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bg11-29 {ECO:0000313|EMBL:PKH51079.1,
RC   ECO:0000313|Proteomes:UP000233844};
RA   Collins E., Ducluzeau A.-L.;
RT   "Pharmacopeia of the Arctic Ocean.";
RL   Submitted (DEC-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:PKH51079.1}.
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DR   EMBL; PJBB01000003; PKH51079.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N1F842; -.
DR   OrthoDB; 9806583at2; -.
DR   Proteomes; UP000233844; Unassembled WGS sequence.
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; 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:UP000233844};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          62..316
FT                   /note="3-dehydroquinate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01761"
SQ   SEQUENCE   352 AA;  39389 MW;  959FE2556722DB09 CRC64;
     MTTIQAVTYP IHFNEKAYNE LTNLIRKNNY SSIFMLVDDN TLEHCYPRFI QLLETDKPIE
     VIQIEAGEIN KNIETCVGVW NAMTELGADR KSLLITLGGG VITDLGGFVA STFKRGIDFI
     NIPTTLLSMV DASVGGKTGV DLGVLKNQIG LFANPEMIVL DPEYLQTLIA REIRSGTAEI
     IKYGMTHDIR LFNEIKDNAD LNIIDLIHRS IEIKNEVVLE DPTEQSIRKV LNWGHTIGHG
     IESHFLESSA KENLTHGEAI AIGIVCEAYI SAELLGFPSD NLQDLKKAII AIYGKVIILE
     EDFSAIMELM KHDKKNVAGE INFVLLKNYE DFKIDCKVPS ELIIDSLKYY NL
//
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