ID A0A0U3PGY4_9ACTN Unreviewed; 200 AA.
AC A0A0U3PGY4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chorismate mutase {ECO:0000256|ARBA:ARBA00012404, ECO:0000256|PIRNR:PIRNR026640};
DE EC=5.4.99.5 {ECO:0000256|ARBA:ARBA00012404, ECO:0000256|PIRNR:PIRNR026640};
GN ORFNames=AS200_13730 {ECO:0000313|EMBL:ALV32998.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32998.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV32998.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32998.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the Claisen rearrangement of chorismate to
CC prephenate. {ECO:0000256|PIRNR:PIRNR026640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5;
CC Evidence={ECO:0000256|PIRNR:PIRNR026640};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis;
CC prephenate from chorismate: step 1/1. {ECO:0000256|ARBA:ARBA00004817,
CC ECO:0000256|PIRNR:PIRNR026640}.
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DR EMBL; CP013743; ALV32998.1; -; Genomic_DNA.
DR RefSeq; WP_058922675.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PGY4; -.
DR STRING; 1725411.AS200_13730; -.
DR KEGG; scx:AS200_13730; -.
DR OrthoDB; 3825510at2; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR008240; Chorismate_mutase_periplasmic.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR NCBIfam; TIGR01806; CM_mono2; 1.
DR PANTHER; PTHR38041; CHORISMATE MUTASE; 1.
DR PANTHER; PTHR38041:SF2; SECRETED CHORISMATE MUTASE; 1.
DR Pfam; PF01817; CM_2; 1.
DR PIRSF; PIRSF026640; Peripl_chor_mut; 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, ECO:0000256|PIRNR:PIRNR026640};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..200
FT /note="Chorismate mutase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006842955"
FT DOMAIN 22..118
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
SQ SEQUENCE 200 AA; 21402 MW; B9C45F71C861A9AC CRC64;
MRTSTPHRTV LTVAAALLAV PGTAAAASAA PRHPADVVRT ADLLRPVAAL AADRLATADL
VAAAKWGTDS PIDDPAREQQ VLDTVAAQAQ QIGADPDETR RVFRDQIEAN KLVQRALFAE
WTAHPDRAPT TKPDLSVVRA TINRINTDLV RSLADTTPER VSPNCGPELL VAAVEVHHEK
HQDLLHTTAL ARSLAHICRG
//
