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Database: UniProt
Entry: A0A1Y3NLM9_PIRSE
LinkDB: A0A1Y3NLM9_PIRSE
Original site: A0A1Y3NLM9_PIRSE 
ID   A0A1Y3NLM9_PIRSE        Unreviewed;       197 AA.
AC   A0A1Y3NLM9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE            EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
DE   Flags: Fragment;
GN   ORFNames=PIROE2DRAFT_3870 {ECO:0000313|EMBL:OUM68425.1};
OS   Piromyces sp. (strain E2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM68425.1, ECO:0000313|Proteomes:UP000195826};
RN   [1] {ECO:0000313|EMBL:OUM68425.1, ECO:0000313|Proteomes:UP000195826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2 {ECO:0000313|EMBL:OUM68425.1,
RC   ECO:0000313|Proteomes:UP000195826};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU363071};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC       Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602480-1};
CC       Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC       manganese, cobalt or cadmium ions. {ECO:0000256|PIRSR:PIRSR602480-1};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|RuleBase:RU363071}.
CC   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
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DR   EMBL; KZ150772; OUM68425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3NLM9; -.
DR   STRING; 73868.A0A1Y3NLM9; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000195826; 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   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002480; DAHP_synth_2.
DR   PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1.
DR   Pfam; PF01474; DAHP_synth_2; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363071};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU363071};
KW   Cadmium {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Manganese {ECO:0000256|PIRSR:PIRSR602480-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195826};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT   BINDING         24
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         63
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OUM68425.1"
SQ   SEQUENCE   197 AA;  22556 MW;  25DB7E38551B94B1 CRC64;
     IEKLKEQLRE VAENKRFLLQ GGDCAELFEY CNKDNIENQL KILLKQSLIL IWGGRTSVVR
     IGRMAGQYAK PRSSPVEVID GKEYPSYRGD IVNGYEIDDR EPDPDRLLQS YFHSSATLNY
     IRSLINTGFA DLHKAEHWNL SHIRNQTLRV EHEAIIDQLR TSLEFLNIVG LNKNSNPSLE
     TIDFFVSHEG LLLDVSG
//
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