ID G7VXI0_PAETH Unreviewed; 361 AA.
AC G7VXI0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase {ECO:0000313|EMBL:AET59422.1};
GN OrderedLocusNames=HPL003_13355 {ECO:0000313|EMBL:AET59422.1};
OS Paenibacillus terrae (strain HPL-003).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=985665 {ECO:0000313|EMBL:AET59422.1, ECO:0000313|Proteomes:UP000005876};
RN [1] {ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|Proteomes:UP000005876};
RA Shin S.H., Kim S., Kim J.Y.;
RT "Complete sequence of Paenibacillus terrae HPL-003.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HPL-003;
RA Shin S.H., Kim S., Kim J.Y.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AET59422.1, ECO:0000313|Proteomes:UP000005876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPL-003 {ECO:0000313|EMBL:AET59422.1,
RC ECO:0000313|Proteomes:UP000005876};
RX PubMed=22328761; DOI=10.1128/JB.06668-11;
RA Shin S.H., Kim S., Kim J.Y., Song H.Y., Cho S.J., Kim D.R., Lee K.I.,
RA Lim H.K., Park N.J., Hwang I.T., Yang K.S.;
RT "Genome Sequence of Paenibacillus terrae HPL-003, a Xylanase-Producing
RT Bacterium Isolated from Soil Found in Forest Residue.";
RL J. Bacteriol. 194:1266-1266(2012).
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DR EMBL; CP003107; AET59422.1; -; Genomic_DNA.
DR RefSeq; WP_014280149.1; NC_016641.1.
DR AlphaFoldDB; G7VXI0; -.
DR STRING; 985665.HPL003_13355; -.
DR KEGG; pta:HPL003_13355; -.
DR eggNOG; COG2876; Bacteria.
DR HOGENOM; CLU_062599_1_0_9; -.
DR OrthoDB; 9780456at2; -.
DR Proteomes; UP000005876; Chromosome.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProt.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR010954; Chorismate_mutase_GmP-bac.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006268; DAHP_syn_2.
DR NCBIfam; TIGR01801; CM_A; 1.
DR NCBIfam; TIGR01361; DAHP_synth_Bsub; 1.
DR PANTHER; PTHR43018; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR PANTHER; PTHR43018:SF1; PROTEIN AROA(G); 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 4: Predicted;
FT DOMAIN 2..92
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
SQ SEQUENCE 361 AA; 39882 MW; 6DC2DBD85383ED6F CRC64;
MSTNENSLEL LREQLDATNL QLLELLSQRA ELAGQLGKLK EAQGVPDFDP VREQQMLDKL
IAANRGPFDD ATIRQLFKNI FKASLNYQKE EHKKHLIVSR KNQPDSTVIK VKDTLVGGKA
SVMVAGPCSV ESYQQTREVG EALKEAGVPI LRGGAFKPRT SPYDFQGLGV EGLQILKRVG
DELGLATISE IVDPRHLEEA IQYIDIIQIG ARNMHNFELL KAAGETRTPI LLKRGLAATM
EEFLHAAEYI VSRGNTQVML IERGIRTYEK WTRNTLDISA VPILKKESHL PVLVDVTHST
GRKDILAPCA KAALAAGADG IMVEVHPNPA VALSDAQQQL NIPEFHNFLS EVKESGLFKV
K
//
