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Entry: A0A1E8FS57_9MICC
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ID   A0A1E8FS57_9MICC        Unreviewed;       456 AA.
AC   A0A1E8FS57;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BIU82_17170 {ECO:0000313|EMBL:OFI38795.1};
OS   Arthrobacter sp. SW1.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1920889 {ECO:0000313|EMBL:OFI38795.1, ECO:0000313|Proteomes:UP000176251};
RN   [1] {ECO:0000313|EMBL:OFI38795.1, ECO:0000313|Proteomes:UP000176251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW1 {ECO:0000313|EMBL:OFI38795.1,
RC   ECO:0000313|Proteomes:UP000176251};
RA   Shaligram S.M., Kumbhare S.V., Pawar S., Dhotre D., Muddeshwar M.G.,
RA   Kapley A.;
RT   "Genomic insights of Arthrobacter sp. strain SW1 for secondary metabolite
RT   production.";
RL   Submitted (SEP-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|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|RuleBase:RU363071}.
CC   -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00008911, ECO:0000256|RuleBase:RU363071}.
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:OFI38795.1}.
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DR   EMBL; MJLT01000009; OFI38795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E8FS57; -.
DR   STRING; 1920889.BIU82_17170; -.
DR   OrthoDB; 9766852at2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000176251; 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   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   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:UP000176251};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT   BINDING         81
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         120
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         276..277
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         299
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         330
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         362
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         404
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT   BINDING         434
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ   SEQUENCE   456 AA;  50157 MW;  D74AF1BED5314475 CRC64;
     MTGPMTSTAQ SGAADYPGLD DWRELPISQQ PTWADKDVFD ASVKELSVLP PLVFAGEVDI
     LRERLAAAAQ GRAFLLQGGD CAETFEGATA DKISARVKTI LQMAVVLTYG AAMPVIKMGR
     MAGQFAKPRS SNEETRDGVT LPAYRGDIVN GYDFTPESRA HDAGRMLKAY HTSASTLNLI
     RAFTQGGFAD LRLVHQWNKG FTENPAHARY ESLARDIDRA IRFMDSCGAD FEALKRVEFF
     ASHEALLLDY ERALTRIDSR TGLPYDTSGH FLWIGERTRE LDHAHVDFLS RVRNPIGVKL
     GPGTSGDDAL RLIDKLDPNR EPGRLTFITR MGAKNIREKL PAVVERVTAS GAQVLWVTDP
     MHGNTVTSPN GYKTRNFDDV IDEVRGFFEV HQSLGTVPGG LHVEMTGDDV AECLGGADPI
     DQDAFLDRYE SVCDPRLNHM QSLEMAFLVA GALAKH
//
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