ID   AROG_CANAL              Reviewed;         370 AA.
AC   P79023; A0A1D8PDG6; Q59LX7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN   Name=ARO4; OrderedLocusNames=CAALFM_C105110CA;
GN   ORFNames=CaO19.11542, CaO19.4060;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11651 / B792 / 171D;
RA   Sousa S., Pereira S.A., Livi G.P.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RX   PubMed=8625423; DOI=10.1007/bf02221512;
RA   Pereira S.A., Livi G.P.;
RT   "Aromatic amino-acid biosynthesis in Candida albicans: identification of
RT   the ARO4 gene encoding a second DAHP synthase.";
RL   Curr. Genet. 29:441-445(1996).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP).
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   -!- ACTIVITY REGULATION: Inhibited by tyrosine. {ECO:0000250}.
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; U53216; AAB48240.1; -; Genomic_DNA.
DR   EMBL; CP017623; AOW26182.1; -; Genomic_DNA.
DR   PIR; S68093; S68093.
DR   RefSeq; XP_710729.1; XM_705637.2.
DR   AlphaFoldDB; P79023; -.
DR   SMR; P79023; -.
DR   STRING; 237561.P79023; -.
DR   PRIDE; P79023; -.
DR   GeneID; 3647668; -.
DR   KEGG; cal:CAALFM_C105110CA; -.
DR   CGD; CAL0000182853; ARO4.
DR   VEuPathDB; FungiDB:C1_05110C_A; -.
DR   eggNOG; ENOG502QPSU; Eukaryota.
DR   HOGENOM; CLU_030903_0_1_1; -.
DR   InParanoid; P79023; -.
DR   OMA; VMENVAN; -.
DR   OrthoDB; 1034517at2759; -.
DR   UniPathway; UPA00053; UER00084.
DR   PRO; PR:P79023; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IGI:CGD.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..370
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase,
FT                   tyrosine-inhibited"
FT                   /id="PRO_0000140850"
SQ   SEQUENCE   370 AA;  40291 MW;  11E5E324C8D7B6DB CRC64;
     MSKTPVPTEY DDTRILGYDP LVPPALLQHE IKASAESLDV VIKGRYDSAQ ILKGNDDRCI
     VIVGPCSIHD PPQALEYGKR LKKLADELKD DLVIIMRAYL EKPRTTVGWK GLINDPDVDN
     SFDINRGLKI SRQLYSDLTS VVGLPIGSEM LDTISPQYFS DFLSFGAIGA RTTESQLHRE
     LASGLSFPIG FKNGTDGGLA VALDAVQASS KGHHFMGVTK NGMAAITTTK GNDCCFIILR
     GGKKITNYDV ESVKAAKEAI AKCTDPSIKL MVDCSHDNSR KDYRNQPQVL DSVAEQISNG
     EDSIIGVMIE SNIHEGKQPM PPAGSGKEAL KYGVSITDGC VSWETTVEML TKLSQAVQTR
     RSLKKQKVSN