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Database: UniProt
Entry: M1WR15_PSEP2
LinkDB: M1WR15_PSEP2
Original site: M1WR15_PSEP2 
ID   M1WR15_PSEP2            Unreviewed;       354 AA.
AC   M1WR15;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Chorismate synthase {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300};
DE            Short=CS {ECO:0000256|HAMAP-Rule:MF_00300};
DE            EC=4.2.3.5 {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|HAMAP-Rule:MF_00300};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000256|HAMAP-Rule:MF_00300};
GN   Name=aroC {ECO:0000256|HAMAP-Rule:MF_00300,
GN   ECO:0000313|EMBL:CCH48032.1};
GN   OrderedLocusNames=BN4_10795 {ECO:0000313|EMBL:CCH48032.1};
OS   Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS   (Desulfovibrio piezophilus).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH48032.1, ECO:0000313|Proteomes:UP000011724};
RN   [1] {ECO:0000313|EMBL:CCH48032.1, ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA   Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA   Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA   Ollivier B., Dolla A.;
RT   "The first genomic and proteomic characterization of a deep-sea sulfate
RT   reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT   piezophilus.";
RL   PLoS ONE 8:e55130-e55130(2013).
RN   [2] {ECO:0000313|Proteomes:UP000011724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
CC   -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and
CC       the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to
CC       yield chorismate, which is the branch point compound that serves as the
CC       starting substrate for the three terminal pathways of aromatic amino
CC       acid biosynthesis. This reaction introduces a second double bond into
CC       the aromatic ring system. {ECO:0000256|HAMAP-Rule:MF_00300}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC         phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00300,
CC         ECO:0000256|RuleBase:RU000605};
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00300,
CC         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 biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       7/7. {ECO:0000256|ARBA:ARBA00005044, 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|ARBA:ARBA00008014, ECO:0000256|HAMAP-Rule:MF_00300,
CC       ECO:0000256|RuleBase:RU000605}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00300}.
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DR   EMBL; FO203427; CCH48032.1; -; Genomic_DNA.
DR   RefSeq; WP_015414086.1; NC_020409.1.
DR   AlphaFoldDB; M1WR15; -.
DR   STRING; 1322246.BN4_10795; -.
DR   KEGG; dpi:BN4_10795; -.
DR   PATRIC; fig|879567.3.peg.820; -.
DR   eggNOG; COG0082; Bacteria.
DR   HOGENOM; CLU_034547_0_2_7; -.
DR   OMA; MLSINAV; -.
DR   OrthoDB; 9771806at2; -.
DR   BioCyc; DPIE1322246:BN4_RS04075-MONOMER; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000011724; Chromosome.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07304; Chorismate_synthase; 1.
DR   Gene3D; 3.60.150.10; Chorismate synthase AroC; 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   NCBIfam; TIGR00033; aroC; 1.
DR   PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR   PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR   Pfam; PF01264; Chorismate_synt; 1.
DR   PIRSF; PIRSF001456; Chorismate_synth; 1.
DR   SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR   PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR   PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00300};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00300}; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00300};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00300};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011724}.
FT   BINDING         48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT   BINDING         126..128
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT   BINDING         278
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT   BINDING         293..297
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
FT   BINDING         319
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   354 AA;  37388 MW;  CB6E7D641BFCD3CD CRC64;
     MHGNIFGEIF TLSTFGESHG PGLGGIIDGC PSGIPLDESM LQLELDRRKP GQGGIASTAR
     QEADHVRILS GVFEGMTTGT PIGFTVENTD QRSRDYSKIK DVFRPGHADF TLNGKFGFRD
     YRGGGRSSGR ETVSRVAGGA VAQELLRSEG IAIFAYTVEL GGIAADILDF EGAQDRPYFS
     PDPKAPALWE ERIKDVKSQG DTLGGVVEVR ATSVPVGLGE PVFGKLDARL AHALMSVGAV
     KGVEIGSGMQ AARSLGSENN DAIGPEGFLS NNSGGVLGGI SSGQDIVARA YIKPIPSISR
     EQQTVTTHGE PTRINIGGRH DIAAIPRINP VLKAMMALTI ADLLLLDRRL GVRA
//
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