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Entry: A0A1Y6E9E4_9SPHN
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ID   A0A1Y6E9E4_9SPHN        Unreviewed;       457 AA.
AC   A0A1Y6E9E4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE            EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
GN   ORFNames=SAMN06297468_0239 {ECO:0000313|EMBL:SMQ59129.1};
OS   Altererythrobacter xiamenensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ59129.1, ECO:0000313|Proteomes:UP000194420};
RN   [1] {ECO:0000313|Proteomes:UP000194420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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|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   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
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DR   EMBL; FXWG01000001; SMQ59129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6E9E4; -.
DR   OrthoDB; 9766852at2; -.
DR   Proteomes; UP000194420; Unassembled WGS sequence.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002480; DAHP_synth_2.
DR   NCBIfam; TIGR01358; DAHP_synth_II; 1.
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   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:UP000194420};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT   BINDING         69
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         108
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         291
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         322
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         396
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         426
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ   SEQUENCE   457 AA;  50346 MW;  04BC867AD652D1F5 CRC64;
     MAQNWTPDGW KAHEARHLPH YEDADELAQA EETLASYPPL VFAGEARALK ADLAEVAAGH
     AFLLQGGDCA ESFAEFHPNN IRDTFRVLLQ MAVVMTFASK RPVVKVGRMA GQFAKPRSSP
     TETQGDLTLP SYFGDNINGI DFDPEQRRND PMRMVRAYSQ AAATLNLLRA FAGGGYANLR
     QVHQWTLDFM GRTPWAEKFA ETADRIGEAL DFMEACGVDP ATVPQLQGTS FYTSHEGLLL
     PYEQALTRQD SLTGDWYATS AHMLWIGDRT RFDGSAHVEF ARGIGNPLGM KCGPSLAPDD
     LLRMLDTLNP GREPGRMTLI SRFGHDKVEE GLPPLVRAVE REGHPVVWSC DPMHGNVVKS
     DSGYKTRPFD RILKEVKGFF AVHRAEGTHP GGIHIEMTGQ DVTECVGGAV AITDDALGDR
     YHTHCDPRLN AAQSLELAFL IAEMLNDEIG ERRADAA
//
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