ID A0A1X1BT79_9GAMM Unreviewed; 180 AA.
AC A0A1X1BT79;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=HA41_15055 {ECO:0000313|EMBL:ORM51541.1};
OS Pantoea conspicua.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=472705 {ECO:0000313|EMBL:ORM51541.1, ECO:0000313|Proteomes:UP000193933};
RN [1] {ECO:0000313|EMBL:ORM51541.1, ECO:0000313|Proteomes:UP000193933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24534 {ECO:0000313|EMBL:ORM51541.1,
RC ECO:0000313|Proteomes:UP000193933};
RX PubMed=28255640;
RA Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT "Phylogenomic resolution of the bacterial genus Pantoea and its
RT relationship with Erwinia and Tatumella.";
RL Antonie Van Leeuwenhoek 0:0-0(2017).
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}.
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:ORM51541.1}.
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DR EMBL; MLFN01000049; ORM51541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1BT79; -.
DR OrthoDB; 8445094at2; -.
DR UniPathway; UPA00120; UER00203.
DR Proteomes; UP000193933; Unassembled WGS sequence.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..180
FT /note="Chorismate mutase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013389689"
FT DOMAIN 10..102
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
SQ SEQUENCE 180 AA; 20132 MW; 8D26E65F52D5F0CA CRC64;
MTQCMAFFFS SLFMCSNVFA GSVSSVSLGA LSTALNERMQ VMKQVAGYKA LHHLPVEDLP
REQAVLENML ENARQAGLEP HSVEPFVHAL MNASKAVQYR YRADWLSTPD NQPVRDLADT
RQQIQRLDNQ LLTAISQYLM ASAFSQDDSA WLLTQLTAPL LSEADKNSLM AALARIQRMH
//
