ID A0A199AX70_9ACTN Unreviewed; 468 AA.
AC A0A199AX70;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AYO52_11265 {ECO:0000313|EMBL:OAV78761.1};
OS Dietzia sp. 111N12-1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=1785156 {ECO:0000313|EMBL:OAV78761.1, ECO:0000313|Proteomes:UP000092558};
RN [1] {ECO:0000313|EMBL:OAV78761.1, ECO:0000313|Proteomes:UP000092558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=111N12-1 {ECO:0000313|EMBL:OAV78761.1,
RC ECO:0000313|Proteomes:UP000092558};
RA Yu M.;
RT "Draft genome sequence of Dietzia sp.111N12-1 isolated from South China Sea
RT with petroleum hydrocarbons degradation activity.";
RL Submitted (FEB-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:OAV78761.1}.
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DR EMBL; LSSV01000023; OAV78761.1; -; Genomic_DNA.
DR RefSeq; WP_067713735.1; NZ_LSSV01000023.1.
DR AlphaFoldDB; A0A199AX70; -.
DR STRING; 1785156.AYO52_11265; -.
DR GeneID; 84687480; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000092558; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 127
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 289..290
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 312
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 343
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 375
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 417
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 447
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 468 AA; 50872 MW; 9CA3096D1E93D279 CRC64;
MSNWTVDVDI AQLPDLPPLS ADLDRQLADA LSRPALQQPS WDPGHAAAMR KVLESVPPIC
VASEVEHLSD RLADVAHGRA FLLQGGDCAE TFEANTEPHI KGVIRTLLQM SVVLTYGASM
PVVKVGRIAG QYAKPRSADR DGTGLLSYRG DMVNALEPDE AAREHDASRL VRAYANAAAA
MNLVRSLTAS GTADLHRVHE WNMEFVAGSP AGARYEALAA EVDRGLRFMD ACGVSDQNLR
SADIFSSHEA LVLDYERAML RLADDGTGLT GDAEQGLYDL SAHFLWIGER TRGIDDAHVA
FASLIQNPIG LKIGPTTTPE LAVEYVEKLD PHNRPGRLTL VSRMGNDKVR DALPPIVQAV
EATGHKVIWQ CDPMHGNTHS TSNGYKTRHF DRIIDEVQGF FEVHHALGSH PGGIHIELTG
EDVTECLGGA QDISDIDLAG RYETACDPRL NTQQSLELAY LVAEMLRS
//
