ID A0A077KQ23_9FLAO Unreviewed; 348 AA.
AC A0A077KQ23;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00017684};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN ORFNames=CHSO_2542 {ECO:0000313|EMBL:BAP31579.1};
OS Chryseobacterium sp. StRB126.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=878220 {ECO:0000313|EMBL:BAP31579.1, ECO:0000313|Proteomes:UP000031650};
RN [1] {ECO:0000313|EMBL:BAP31579.1, ECO:0000313|Proteomes:UP000031650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StRB126 {ECO:0000313|EMBL:BAP31579.1,
RC ECO:0000313|Proteomes:UP000031650};
RX PubMed=25291777; DOI=10.1128/genomeA.00952-14;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Complete Genome Sequence of Chryseobacterium sp. Strain StRB126, an N-
RT Acylhomoserine Lactone-Degrading Bacterium Isolated from Potato Root.";
RL Genome Announc. 2:e00952-14(2014).
CC -!- FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate
CC 7-phosphate (DAHP) to dehydroquinate (DHQ).
CC {ECO:0000256|ARBA:ARBA00003485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-
CC dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001393};
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 -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 2/7. {ECO:0000256|ARBA:ARBA00004661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the sugar phosphate cyclases superfamily.
CC Dehydroquinate synthase family. {ECO:0000256|ARBA:ARBA00005412}.
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DR EMBL; AP014624; BAP31579.1; -; Genomic_DNA.
DR RefSeq; WP_045496635.1; NZ_AP014624.1.
DR AlphaFoldDB; A0A077KQ23; -.
DR KEGG; chz:CHSO_2542; -.
DR HOGENOM; CLU_001201_0_1_10; -.
DR OrthoDB; 9806583at2; -.
DR Proteomes; UP000031650; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; 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: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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 53..308
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
SQ SEQUENCE 348 AA; 39569 MW; 8FB673C99E91993C CRC64;
MITILNDNFS QLNTFLHENT FSKIFILVDE NTHEYCLPVL LGNMETDLGF EILEIEAGEE
MKNIQTANQL WEILTEMQAD RKALVINLGG GVITDMGGFV ASTYKRGIKF INIPTTLLSM
CDASIGGKTG IDLMHYKNMV GTFAFPEQIF IYPKFLETLP FKELRSGFAE MLKHGLIADK
AHWNQLIQLH KLDVEAVTPY IQNSMDIKQD VVEKDFHESN IRKTLNFGHT IGHAVESLCL
QQENPILHGE AVAMGMICEA HLAYLENLIS EEDSKTIIEN IQRYYPYLDI SDFKDEDITA
LLLNDKKNVD SKINFSLLTG IGECNYDYQC SQKNIIESLS FYRKLNDA
//
