ID   N4WHY5_9BACI            Unreviewed;       353 AA.
AC   N4WHY5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase {ECO:0000313|EMBL:ENH95787.1};
GN   ORFNames=J416_14168 {ECO:0000313|EMBL:ENH95787.1};
OS   Gracilibacillus halophilus YIM-C55.5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH95787.1, ECO:0000313|Proteomes:UP000012283};
RN   [1] {ECO:0000313|EMBL:ENH95787.1, ECO:0000313|Proteomes:UP000012283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH95787.1,
RC   ECO:0000313|Proteomes:UP000012283};
RA   Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT   "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT   halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:ENH95787.1}.
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; APML01000074; ENH95787.1; -; Genomic_DNA.
DR   RefSeq; WP_003473642.1; NZ_APML01000074.1.
DR   AlphaFoldDB; N4WHY5; -.
DR   STRING; 1308866.J416_14168; -.
DR   PATRIC; fig|1308866.3.peg.2855; -.
DR   eggNOG; COG2876; Bacteria.
DR   OrthoDB; 9780456at2; -.
DR   Proteomes; UP000012283; 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;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012283}.
FT   DOMAIN          1..91
FT                   /note="Chorismate mutase"
FT                   /evidence="ECO:0000259|PROSITE:PS51168"
FT   COILED          6..33
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   353 AA;  39275 MW;  53424288EDCEF8C8 CRC64;
     MSNEQLDQLR EKLDNINLEI LDLVNQRAEL VKETGQVKEK QGANRNYDPV RERDMLDLIT
     KHNDGPFENS TIVHLFKEIF KAGLELQEDD HSKALLVSRK KKPEDTVIEI NGEKFGDGDP
     HFIFGPCSVE SYDQVAEVAK AVKEQGFHLI RGGAFKPRTS PYDFQGLGFE GLEILKQISN
     EYGLSVVSEI VNPAHIEEAA DYIDVIQIGA RNMQNFELLK AAGETNKPVL LKRGMSATIS
     DFINAAEYIN SKGNGDIILC ERGIRTYEKA TRNTLDITAV PILKQETHLP VMVDVTHSTG
     RRDLLLPAAK AALAIGADGV MAEVHPDPAV ALSDSAQQMD IPTFHQFMEN LRK
//