ID K8ENB3_9CHLO Unreviewed; 465 AA.
AC K8ENB3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=3-dehydroquinate synthase {ECO:0000256|ARBA:ARBA00013031};
DE EC=4.2.3.4 {ECO:0000256|ARBA:ARBA00013031};
GN OrderedLocusNames=Bathy14g03440 {ECO:0000313|EMBL:CCO19732.1};
OS Bathycoccus prasinos.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Bathycoccus.
OX NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO19732.1, ECO:0000313|Proteomes:UP000198341};
RN [1] {ECO:0000313|EMBL:CCO19732.1, ECO:0000313|Proteomes:UP000198341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO19732.1,
RC ECO:0000313|Proteomes:UP000198341};
RA Genoscope - CEA;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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=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}.
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DR EMBL; FO082265; CCO19732.1; -; Genomic_DNA.
DR RefSeq; XP_007509275.1; XM_007509213.1.
DR AlphaFoldDB; K8ENB3; -.
DR STRING; 41875.K8ENB3; -.
DR GeneID; 19011810; -.
DR KEGG; bpg:Bathy14g03440; -.
DR eggNOG; KOG0692; Eukaryota.
DR OrthoDB; 865at2759; -.
DR Proteomes; UP000198341; Chromosome_14.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
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 HAMAP; MF_00110; DHQ_synthase; 1.
DR InterPro; IPR016037; DHQ_synth_AroB.
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 SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000198341}.
FT DOMAIN 160..423
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 51853 MW; 46047F98BD4CCEAA CRC64;
MRFFSSLSLS SCASCSCSSR RGLTSSSSSF TSSSTFSRRR QNRRRRRRRT NEKNAKTTTT
LISNDAKEND NDDNDNNNNN RRKEPDAIVS VKLDQDGQRD YPIYIGSELV KERGDLLRKH
IKGETVLIVT NETVAPLYLE KVKESLLLSS SSKSLRIESV VLPDGEEHKN LDVLDLIFEK
ALDARLDRKT TFIALGGGVI GDMTGFAASA YQRGVNFIQI PTTVMAMVDS SVGGKTGVNH
KKGKNMIGAF YQPQCVFVDI DSLDSLPERE YNSGIAEVIK YGLIRDAKFF DWIEQNADKL
QKKAIDRKSL VYAIQRSCEN KAEVVELDEK ESGLNVRATL NLGHTFGHAI ETGVGYGEYL
HGEAVSIGTA MAADLSFRLG WIDENLQTRT VDLLKRFDLP IEVPRGSMTK EKFMDLMAVD
KKASQGKMNF ILLKGDLGGC VFTGDFDQTK LRETLESFVD GRISR
//