ID A0A0E3YZF5_9GAMM Unreviewed; 464 AA.
AC A0A0E3YZF5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=WQ53_03620 {ECO:0000313|EMBL:AKC85989.1};
OS Pseudoxanthomonas suwonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC85989.1, ECO:0000313|Proteomes:UP000033067};
RN [1] {ECO:0000313|EMBL:AKC85989.1, ECO:0000313|Proteomes:UP000033067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J1 {ECO:0000313|EMBL:AKC85989.1,
RC ECO:0000313|Proteomes:UP000033067};
RX PubMed=26067962;
RA Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL Genome Announc. 3:e00614-15(2015).
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; CP011144; AKC85989.1; -; Genomic_DNA.
DR RefSeq; WP_052630503.1; NZ_CP011144.1.
DR AlphaFoldDB; A0A0E3YZF5; -.
DR KEGG; psuw:WQ53_03620; -.
DR PATRIC; fig|314722.6.peg.758; -.
DR eggNOG; COG3200; Bacteria.
DR OrthoDB; 9766852at2; -.
DR Proteomes; UP000033067; Chromosome.
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:UP000033067};
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 301
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 332
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 406
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 436
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 464 AA; 51787 MW; C2C10ABDA8B41F88 CRC64;
MSTPERSLQP VNLADGWSPA SWRGRPALQM PQYPDPSALE AALAELRQLP PLVTSWEIFA
LKKQIAEAQE GQRFLLQGGD CAENFSDCES GTISNRLKVL LQMSLVLVHG LRLPVVRVGR
FAGQYAKPRS TDLETRGEVS LPSYRGDVVN GPEFTAQARV PDPRRMLTAH ARSAMTMNFV
RALIDGGFAD LHHPEYWSLS WVGCSPLAED YQKMVNSIGD AVRFMETLAG VEVHNLNRID
FYTSHEALLL PYEEALTRQV PRQWGWFNLS THYPWIGMRT AALDGAHVEY FRGIRNPVAI
KVGPSVQPDQ LLRLIDVLNP DDEPGRLTFI HRMGAAQIAS KLPPLLEAVR RDGRRVLWVC
DAMHGNTEST ANGYKTRRFA NILAEVEQSF DLHAAAGTRL GGVHLELTGE DVTECTGGAR
ELTEVDLERA YRSTVDPRLN YEQSLEIAMA IVRKQGQRQA DARV
//
