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Entry: N4VHE1_COLOR
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ID   N4VHE1_COLOR            Unreviewed;       375 AA.
AC   N4VHE1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   Name=AMT16 {ECO:0000313|EMBL:TDZ17736.1};
GN   ORFNames=Cob_v009336 {ECO:0000313|EMBL:TDZ17736.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ17736.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
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         ECO:0000256|PIRNR:PIRNR001361};
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
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:TDZ17736.1}.
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DR   EMBL; AMCV02000027; TDZ17736.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4VHE1; -.
DR   STRING; 1213857.N4VHE1; -.
DR   EnsemblFungi; ENH87493; ENH87493; Cob_04314.
DR   eggNOG; ENOG502QPSU; Eukaryota.
DR   HOGENOM; CLU_030903_0_1_1; -.
DR   OrthoDB; 72311at2759; -.
DR   Proteomes; UP000014480; 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:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF18; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHENYLALANINE-INHIBITED; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          57..354
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   375 AA;  40620 MW;  BCAE97614FA71C08 CRC64;
     MSSFYIENKS VGNKAESEDW RIRGYNPLTP PDLLQHEIAQ TAKSKQTVID GREEAAAIVN
     GTDEKGRLLV IIGPCSIHDP KAALEYCDLL LAAKEKHKDE LLIVMRSYLE KPRTTVGWKG
     LINDPDIDNS FKINKGLRLS RQLFVDLTDK GMPIASEMLD TISPQFLADL LSVGAVGART
     TESQLHRELA SGLSFPVGFK NGTDGSLGVA IDAIGAVRHP HHFLSVTKPG VVAIVGTVGN
     EDCFVILRGG TKGTNYDAKS ITEAKAALEK TGLPKRLMVD CSHGNSLKNH KNQPKVAADL
     AEQIAKGETG IMGLMIESNI NEGNQKVPKE GKEGLKYGVS ITDACIHWDD TVSVLDQLAD
     AVKQRREVLG RNGHA
//
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