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Database: UniProt
Entry: A0A2M9BU25_9MICO
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ID   A0A2M9BU25_9MICO        Unreviewed;       382 AA.
AC   A0A2M9BU25;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   ORFNames=CLV54_2402 {ECO:0000313|EMBL:PJJ61457.1};
OS   Compostimonas suwonensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Compostimonas.
OX   NCBI_TaxID=1048394 {ECO:0000313|EMBL:PJJ61457.1, ECO:0000313|Proteomes:UP000230161};
RN   [1] {ECO:0000313|EMBL:PJJ61457.1, ECO:0000313|Proteomes:UP000230161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25625 {ECO:0000313|EMBL:PJJ61457.1,
RC   ECO:0000313|Proteomes:UP000230161};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP). {ECO:0000256|ARBA:ARBA00003726,
CC       ECO:0000256|PIRNR:PIRNR001361}.
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|ARBA:ARBA00001370,
CC         ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
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:PJJ61457.1}.
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DR   EMBL; PGFB01000004; PJJ61457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9BU25; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000230161; 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; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230161};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          65..359
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   382 AA;  40954 MW;  E52C28CCE5DB16B1 CRC64;
     MPFVFNRRVG SGPVRRERIR RMSSTNDLRV TSFEALPSPA ELRDELPLTA AHQDLVSASR
     AAVEAIVRGD DDRLLVVVGP CSVHDPVAAL EYARRLAPIA QRHNDRLLIV MRVYFEKPRS
     TGGWKGLIND PYLDGSHRVA DGLRIARKLL LDILDLGLPV GCEFLEPTSP QYIADTVSWG
     AIGARTTESQ IHRQLASGLS MPIGFKNATD GDVQVAVDGC TVASQSHVFF GVDDDGAASV
     VTTTGNTAAH VILRGGRGGP NYTTPDLAAA ARLLAAAGRP ARLVVDASHA NSGKDHVRQA
     AVVRELAGQI AAGEPIAGLM MESFLVEGAQ KLDGRPLDQL TFGQSVTDAC LGWETTEELL
     LELVEGLMVD PDHRNEELTP AV
//
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