ID A0A126RKZ9_9SPHN Unreviewed; 456 AA.
AC A0A126RKZ9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=K426_06595 {ECO:0000313|EMBL:AMK22265.1};
OS Sphingobium sp. TKS.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK22265.1, ECO:0000313|Proteomes:UP000060779};
RN [1] {ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA Tabata M.;
RT "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium sp.
RT TKS.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK22265.1, ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|EMBL:AMK22265.1,
RC ECO:0000313|Proteomes:UP000060779};
RX PubMed=27056231;
RA Tabata M., Ohhata S., Kawasumi T., Nikawadori Y., Kishida K., Sato T.,
RA Ohtsubo Y., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane Degrader,
RT Sphingobium sp. Strain TKS, Isolated from a gamma-Hexachlorocyclohexane-
RT Degrading Microbial Community.";
RL Genome Announc. 4:0-0(2016).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP005083; AMK22265.1; -; Genomic_DNA.
DR RefSeq; WP_066555261.1; NZ_CP005083.1.
DR AlphaFoldDB; A0A126RKZ9; -.
DR STRING; 1315974.K426_06595; -.
DR KEGG; spht:K426_06595; -.
DR PATRIC; fig|1315974.3.peg.1382; -.
DR OrthoDB; 9766852at2; -.
DR Proteomes; UP000060779; Chromosome 1.
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; 2.
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:UP000060779};
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 456 AA; 50061 MW; 3A101D647B392484 CRC64;
MAAKWTPESW REHKGIQMPV YRDAQALGAV EAQLSQFPPL VFAGEARNLK AELAKVTAGE
AFLLQGGDCA ESFAEFHPNN IRDTFRVLLQ MAVVLTFASK LPIVKVGRMA GQFAKPRSAD
TETIGGVELP SYRGDNVNDI AFTPEAREPD AQRMIRAYNQ SAATLNLVRA FSTGGYASLD
RVHGWMLDFM GRSPWAAKFE AMADQIGQAL DFMRACGLSP ETVPQLGGTS FYTSHEALLL
PYEQALTRQD SLTGDWYDTS AHMLWIGDRT RFEGSAHVEY LRGIGNPIGM KCGPSLEPDA
LIRLLDILNP SREAGRITLI TRYGHDKIEA GLPKLVRAVL REGHPVVWSC DPMHGNVIKA
ANGYKTRPFD RILAEVRGFF AVHRAEGSFG GGIHAEMTGQ NVTECTGGAV AITDEGLADR
YHTHCDPRLN AAQSLELAFL LAEMLNEELK ERRAAA
//
