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Database: UniProt
Entry: A0A147K6M4_9BACI
LinkDB: A0A147K6M4_9BACI
Original site: A0A147K6M4_9BACI 
ID   A0A147K6M4_9BACI        Unreviewed;       359 AA.
AC   A0A147K6M4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Chorismate mutase {ECO:0000313|EMBL:KUP05517.1};
GN   ORFNames=Q75_11770 {ECO:0000313|EMBL:KUP05517.1};
OS   Bacillus coahuilensis p1.1.43.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP05517.1, ECO:0000313|Proteomes:UP000074108};
RN   [1] {ECO:0000313|EMBL:KUP05517.1, ECO:0000313|Proteomes:UP000074108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX   PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA   Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA   Olmedo-Alvarez G.;
RT   "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT   Phosphorus Acquisition Strategies and Their Regulation.";
RL   Front. Microbiol. 7:58-58(2016).
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:KUP05517.1}.
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DR   EMBL; LDYG01000035; KUP05517.1; -; Genomic_DNA.
DR   RefSeq; WP_059351474.1; NZ_LDYG01000035.1.
DR   AlphaFoldDB; A0A147K6M4; -.
DR   STRING; 1150625.Q75_11770; -.
DR   PATRIC; fig|1150625.3.peg.2505; -.
DR   OrthoDB; 9780456at2; -.
DR   Proteomes; UP000074108; Unassembled WGS sequence.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; 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   PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000074108}.
FT   DOMAIN          1..90
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   COILED          6..40
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   359 AA;  39778 MW;  3300EACB6939BFBB CRC64;
     MSHNELDILR EKVDTLNLQL LELINERAKA AQEIGKIKEK QGMYRFDPVR EREMLNQIIE
     NNKGPFEHST IEHIFKEIFK ANLELQQDDH RKALLVSRKK KPEDTVVSIN GENIGDGTPS
     FIFGPCAVES YEQVAAVAES VKAKGLKLLR GGAFKPRTSP YDFQGLGLEG LKILKKVADE
     YNLAVVSEIV NPADIEKALD YIDVIQIGAR NMQNFELLKA AGAVNKPVLL KRGLAATISE
     FINAAEYIIS QGNGQIILCE RGIRTYEKAT RNTLDISAVP ILKQETHLPV FVDVTHSTGR
     RDLLLPTAKA ALAVGADGVM AEVHPDPAVA LSDSAQQMNI DQFDTFFEEI KKGLFISSK
//
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