ID E4RQ42_LEAB4 Unreviewed; 364 AA.
AC E4RQ42;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=DAHP synthetase I/KDSA {ECO:0000313|EMBL:ADQ16525.1};
GN OrderedLocusNames=Lbys_0765 {ECO:0000313|EMBL:ADQ16525.1};
OS Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS 106382 / 4M15).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Leadbetterella.
OX NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ16525.1, ECO:0000313|Proteomes:UP000007435};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Leadbetterella byssophila DSM 17132.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ16525.1, ECO:0000313|Proteomes:UP000007435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC {ECO:0000313|Proteomes:UP000007435};
RX PubMed=21475582; DOI=10.4056/sigs.1413518;
RA Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Leadbetterella byssophila type strain
RT (4M15).";
RL Stand. Genomic Sci. 4:2-12(2011).
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DR EMBL; CP002305; ADQ16525.1; -; Genomic_DNA.
DR RefSeq; WP_013407577.1; NC_014655.1.
DR AlphaFoldDB; E4RQ42; -.
DR STRING; 649349.Lbys_0765; -.
DR KEGG; lby:Lbys_0765; -.
DR eggNOG; COG1605; Bacteria.
DR eggNOG; COG2876; Bacteria.
DR HOGENOM; CLU_062599_1_1_10; -.
DR OrthoDB; 9780456at2; -.
DR Proteomes; UP000007435; Chromosome.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProt.
DR GO; GO:0009058; P: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; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR006218; DAHP1/KDSA.
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;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007435}.
FT DOMAIN 268..359
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT COILED 267..294
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 364 AA; 40908 MW; 93399CDEFB05977E CRC64;
MKANLNVSPL ESWVNTDGKP LIIAGPCSAE TEEQVLETAE GIARNGYAHI YRAGVWKPRT
RPGSFEGKGE EALPWLQKVK EQTGLKTAVE VATPQHVELA LKYGVDVLWI GARTTVNPFN
VQDLADALKG VDVPVLIKNP VNPDLALWVG AFERIAGAGI TKLGGIHRGF SNAQETKYRN
SPMWQIAVEF KTSFPDIPLI GDPSHMAGKR AYLAELTQRA MDLNYDGLII ESHRNPDEAW
SDASQQLTPD ALGEMLNNIE FRNATYGTDF QSELDRLRAR LDNLDRELME VLASRMAIVE
QLGEYKRDNN VAVLQLDRWK HVHQSRAEWA KSLNLYPEVV EELFKLIHME SIRKQTEVMN
RQTV
//