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Database: UniProt
Entry: A0A0Q4LZF5_9SPHN
LinkDB: A0A0Q4LZF5_9SPHN
Original site: A0A0Q4LZF5_9SPHN 
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
//
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