ID   A0A2N1JQB8_9BACI        Unreviewed;       390 AA.
AC   A0A2N1JQB8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   23-MAY-2018, entry version 2.
DE   RecName: Full=Chorismate synthase {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};
DE            Short=CS {ECO:0000256|HAMAP-Rule:MF_00300};
DE            EC=4.2.3.5 {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300};
GN   Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300};
GN   ORFNames=CWE34_29585 {ECO:0000313|EMBL:PKJ52125.1};
OS   Bacillus sp. SN10.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2056493 {ECO:0000313|EMBL:PKJ52125.1, ECO:0000313|Proteomes:UP000233528};
RN   [1] {ECO:0000313|EMBL:PKJ52125.1, ECO:0000313|Proteomes:UP000233528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN10 {ECO:0000313|EMBL:PKJ52125.1,
RC   ECO:0000313|Proteomes:UP000233528};
RA   Nazipi S.;
RT   "Bacillus sp. isolated from nest material of social spiders.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate
CC       and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate
CC       (EPSP) to yield chorismate, which is the branch point compound
CC       that serves as the starting substrate for the three terminal
CC       pathways of aromatic amino acid biosynthesis. This reaction
CC       introduces a second double bond into the aromatic ring system.
CC       {ECO:0000256|HAMAP-Rule:MF_00300}.
CC   -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate =
CC       chorismate + phosphate. {ECO:0000256|HAMAP-Rule:MF_00300,
CC       ECO:0000256|RuleBase:RU000605}.
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00300, ECO:0000256|RuleBase:RU000605};
CC       Note=Reduced FMN (FMNH(2)). {ECO:0000256|HAMAP-Rule:MF_00300,
CC       ECO:0000256|RuleBase:RU000605};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 7/7. {ECO:0000256|HAMAP-Rule:MF_00300,
CC       ECO:0000256|RuleBase:RU000605}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00300}.
CC   -!- SIMILARITY: Belongs to the chorismate synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00300, ECO:0000256|RuleBase:RU000605}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PKJ52125.1}.
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DR   EMBL; PJCU01000029; PKJ52125.1; -; Genomic_DNA.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000233528; Unassembled WGS sequence.
DR   CDD; cd07304; Chorismate_synthase; 1.
DR   Gene3D; 3.60.150.10; -; 1.
DR   HAMAP; MF_00300; Chorismate_synth; 1.
DR   InterPro; IPR000453; Chorismate_synth.
DR   InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR   InterPro; IPR020541; Chorismate_synthase_CS.
DR   PANTHER; PTHR21085; PTHR21085; 1.
DR   Pfam; PF01264; Chorismate_synt; 1.
DR   PIRSF; PIRSF001456; Chorismate_synth; 1.
DR   SUPFAM; SSF103263; SSF103263; 1.
DR   TIGRFAMs; TIGR00033; aroC; 1.
DR   PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR   PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00300,
KW   ECO:0000256|RuleBase:RU000605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00300,
KW   ECO:0000256|RuleBase:RU000605};
KW   Complete proteome {ECO:0000313|Proteomes:UP000233528};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00300};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00300};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_00300};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00300,
KW   ECO:0000256|RuleBase:RU000605};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     132    134       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     253    254       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     313    317       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING      39     39       NADP. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING      45     45       NADP. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING     298    298       FMN; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING     339    339       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
SQ   SEQUENCE   390 AA;  42482 MW;  B84ABCD0BFFCF55D CRC64;
     MRYITAGESH GPQLTVILEG VPAGLTLAAE HINKELLRRQ KGHGRGRRMQ IETDTVEIVS
     GVRHGMTLGS PITLIVKNDD FKHWTKVMGA EPISEKESKE MKRTITKPRP GHADLNGAIK
     YGHRDIRNVL ERSSARETTV RVAAGAVAKQ ILKELGVEIA GHVLEIGGVK AKHISNLSIE
     EIQTITENSP VRCLDKEVEQ EMMDAIDHAK SSGDSIGGIV EVIAEGMPIG VGSYVHYDRK
     LDAKLAGAIM SINAFKGAEI GVGFEAARQP GSKVHDEILW DEEQGYMRKT NNAGGFEGGM
     TTGMPIVVRG VMKPIPTLYK PLASVDIDTK EAFQASIERS DSCAVPAAGV VAESVVAWEL
     AHALVEQFGK DRMELIQQNI TQHNKYAKEF
//