ID A0A0M0JIU7_9EUKA Unreviewed; 584 AA.
AC A0A0M0JIU7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
GN ORFNames=Ctob_008310 {ECO:0000313|EMBL:KOO26262.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO26262.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000256|ARBA:ARBA00001370};
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985}.
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:KOO26262.1}.
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DR EMBL; JWZX01002875; KOO26262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JIU7; -.
DR OrthoDB; 72311at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 3.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DAHP_synth_1.
DR PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR Pfam; PF00793; DAHP_synth_1; 2.
DR SUPFAM; SSF51569; Aldolase; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..206
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT DOMAIN 361..510
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 565..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 61187 MW; AC83BA289F2331CC CRC64;
MESINQRVLS LRALLPPSCV FEELPGNIAT YTQVIDTRQA IINMVAGKDD RLLVVVGPAG
ATADSSALRA LAAQLSSLSS SLSSELVIVL RADACMSLAT ADQVNKGIRC ARELLLEING
LGVPTAIEFR DTITPQFFAD LLAWANVSAR SEAMRELVSG LSMPVGVRAP SSDVASAVRA
IDISGGAHHF LGVSVEGVCG VVKSTGHPDV LAMLPVDGAA AGDGFVGALR RLHEQRPQTA
LVLELGADDA SVTRACEEIC RDGTLGARLV GVDMRLAVEG ASAGGALNAA RLHALAASVT
KRRRSRLHSL AAATAAAPTE THNLRISAVS PLLPPACLLE ELPRTESSAK VVGDARRGIH
KVLTGASDRL VVLLGPAAVD DPAVALEYGA RLVQLAREVA DELLVVMRVE INTPVTPSTG
PWPGLLFDPA RDGSYEINKG IRQSRELLLQ LNALGLPCAL EFRDTITPQF FADVLAWASV
DAGSEMLREL VSGLSMPIEM ASAVAAAVAA GQPTPCGLSL NSYLLAGAAL VGAPAIRGLS
LTEPCVDWLA TEQIVHTLAA AVRTRRERRG PPVDDDAKKR QRGK
//
