ID C7MCF2_BRAFD Unreviewed; 466 AA.
AC C7MCF2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|RuleBase:RU363071};
DE EC=2.5.1.54 {ECO:0000256|RuleBase:RU363071};
GN OrderedLocusNames=Bfae_14280 {ECO:0000313|EMBL:ACU85259.1};
OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU85259.1, ECO:0000313|Proteomes:UP000001919};
RN [1] {ECO:0000313|EMBL:ACU85259.1, ECO:0000313|Proteomes:UP000001919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX PubMed=21304631; DOI=10.4056/sigs.492;
RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachybacterium faecium type strain
RT (Schefferle 6-10).";
RL Stand. Genomic Sci. 1:3-11(2009).
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}.
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DR EMBL; CP001643; ACU85259.1; -; Genomic_DNA.
DR RefSeq; YP_003154849.1; NC_013172.1.
DR AlphaFoldDB; C7MCF2; -.
DR STRING; 446465.Bfae_14280; -.
DR KEGG; bfa:Bfae_14280; -.
DR PATRIC; fig|446465.5.peg.1421; -.
DR eggNOG; COG3200; Bacteria.
DR HOGENOM; CLU_026885_0_1_11; -.
DR OrthoDB; 9766852at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000001919; Chromosome.
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:UP000001919};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363071}.
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 130
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 286..287
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 309
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 340
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 372
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 414
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
FT BINDING 444
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR602480-1"
SQ SEQUENCE 466 AA; 51407 MW; CB2A1462158301D4 CRC64;
MRVTQFSPDA PARAHAFTLS SADDGLAALG AWREYPRVQQ PVWPDEAERA KVFDDLRAAP
PLVFAGEVDV LRDRIAAAAR GEAFLLAGGD CAETFADSTA DRIRNKIRTI LQMAAVLTYG
ASLPVVKMGR MAGQFAKPRS ADEETRDGLT LPTYRGDAVN EFDFTPEARR PDPSRLWRTY
TTSASTLNLL RAFTGGGFAD LREVHSWNRG FTSGAGYDRY EELAGQIDKA VRFMDAIGAD
FDALKVVEFY ASHEALLLDY EEALARIDSR TGEIYGCSGH LLWIGERTRQ LDGAHVDFMA
RLRNPIGVKL GPTATVDDAL RLIDRLDPER EPGRLTFITR MGAGTIRDRL PALVEGVRDS
GAQVAWVTDP MHGNTITSSN GYKTRRFEDI LDEVVGFFEV HQALGTVPAG LHMELTGDDV
TEVLGGAGEI DEEGLTRRYE TLVDPRLNHQ QSLELAFLVA EMLSRR
//
