ID A0A0Q4LZF5_9SPHN Unreviewed; 103 AA.
AC A0A0Q4LZF5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=chorismate mutase {ECO:0000256|ARBA:ARBA00012404};
DE EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404};
GN ORFNames=ASE97_06070 {ECO:0000313|EMBL:KQN39628.1};
OS Sphingomonas sp. Leaf42.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736219 {ECO:0000313|EMBL:KQN39628.1, ECO:0000313|Proteomes:UP000051880};
RN [1] {ECO:0000313|EMBL:KQN39628.1, ECO:0000313|Proteomes:UP000051880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf42 {ECO:0000313|EMBL:KQN39628.1,
RC ECO:0000313|Proteomes:UP000051880};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN39628.1, ECO:0000313|Proteomes:UP000051880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf42 {ECO:0000313|EMBL:KQN39628.1,
RC ECO:0000313|Proteomes:UP000051880};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN39628.1}.
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DR EMBL; LMLF01000004; KQN39628.1; -; Genomic_DNA.
DR RefSeq; WP_055758370.1; NZ_LMLF01000004.1.
DR AlphaFoldDB; A0A0Q4LZF5; -.
DR PATRIC; fig|1736219.3.peg.1337; -.
DR OrthoDB; 514491at2; -.
DR Proteomes; UP000051880; Unassembled WGS sequence.
DR GO; GO:0016835; F:carbon-oxygen lyase activity; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR008241; Isochorismate_pyruvate-lyase.
DR PANTHER; PTHR38041; CHORISMATE MUTASE; 1.
DR PANTHER; PTHR38041:SF1; CHORISMATE MUTASE; 1.
DR Pfam; PF01817; CM_2; 1.
DR PIRSF; PIRSF029775; Isochor_pyr_lyas; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000051880}.
FT DOMAIN 8..98
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR029775-1"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR029775-1"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR029775-1"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR029775-1"
SQ SEQUENCE 103 AA; 10902 MW; 8B1EE246FBBC605E CRC64;
MTTKILPPAD CTTMAEVRAG VDSLDRELVA LLARRFGYMD AAARIKPDRG AVRDEARKAQ
VIANARAAAV AAGAPEAAIG ELWEALVEAS IAHELARFDA TRG
//