ID G5JHT0_9STAP Unreviewed; 362 AA.
AC G5JHT0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase {ECO:0000313|EMBL:EHJ08266.1};
GN ORFNames=SS7213T_05061 {ECO:0000313|EMBL:EHJ08266.1};
OS Staphylococcus simiae CCM 7213 = CCUG 51256.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=911238 {ECO:0000313|EMBL:EHJ08266.1, ECO:0000313|Proteomes:UP000005413};
RN [1] {ECO:0000313|EMBL:EHJ08266.1, ECO:0000313|Proteomes:UP000005413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 7213 {ECO:0000313|EMBL:EHJ08266.1,
RC ECO:0000313|Proteomes:UP000005413};
RX PubMed=22272658; DOI=10.1186/1471-2164-13-38;
RA Suzuki H., Lefebure T., Pavinski Bitar P., Stanhope M.J.;
RT "Comparative genomic analysis of the genus Staphylococcus including
RT Staphylococcus aureus and its newly described sister species Staphylococcus
RT simiae.";
RL BMC Genomics 13:38-38(2012).
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:EHJ08266.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEUN01000348; EHJ08266.1; -; Genomic_DNA.
DR RefSeq; WP_002463097.1; NZ_AEUN01000348.1.
DR AlphaFoldDB; G5JHT0; -.
DR PATRIC; fig|911238.3.peg.848; -.
DR OrthoDB; 9780456at2; -.
DR Proteomes; UP000005413; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProt.
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; IPR036263; Chorismate_II_sf.
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 SUPFAM; SSF48600; Chorismate mutase II; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
PE 4: Predicted;
FT DOMAIN 1..89
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
SQ SEQUENCE 362 AA; 40466 MW; 089950DD916E8223 CRC64;
MTSKLEGYRD EVVKLNHQIL DLLSKRGELA QKIGEEKLKQ GTRIYDPQRE KEMLNDLIDK
NQGPFNDNTI KQLFKEIFKA STDLQKSENE KHLYVSRKLK PEDTIVKFDN GGIIGDGNKS
FVFGPCSVES QEQVDAVAAN LQAKGEKFIR GGAFKPRTSP YDFQGLGVEG LKILKNVKDK
YNLNVVSEIV NPKDFEIADE YLDVFQIGAR NMQNFELLKE AGRTNKPILL KRGLSATIEE
FVFAAEYIAA QGNQNIILCE RGIRTYEKAT RNTLDISAVP ILKQGTHLPV MVDVTHSTGR
KDIMLPTAKA ALAVGADGVM AEVHPDPSVA LSDAGQQMDL NEFQAFYDEI KPLADLYNQN
KL
//
