(data stored in ACNUC7421 zone)

SWISSPROT: AROC_ANADF

ID   AROC_ANADF              Reviewed;         381 AA.
AC   A7H6S8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300};
DE            Short=CS {ECO:0000255|HAMAP-Rule:MF_00300};
DE            EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300};
GN   Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300};
GN   OrderedLocusNames=Anae109_0206;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
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:0000255|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:0000255|HAMAP-Rule:MF_00300};
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00300};
CC       Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       7/7. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00300}.
CC   -!- SIMILARITY: Belongs to the chorismate synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00300}.
DR   EMBL; CP000769; ABS24424.1; -; Genomic_DNA.
DR   RefSeq; WP_011984530.1; NC_009675.1.
DR   SMR; A7H6S8; -.
DR   STRING; 404589.Anae109_0206; -.
DR   PRIDE; A7H6S8; -.
DR   EnsemblBacteria; ABS24424; ABS24424; Anae109_0206.
DR   KEGG; afw:Anae109_0206; -.
DR   eggNOG; ENOG4105D10; Bacteria.
DR   eggNOG; COG0082; LUCA.
DR   HOGENOM; HOG000060334; -.
DR   KO; K01736; -.
DR   OMA; MLSINAV; -.
DR   OrthoDB; 981870at2; -.
DR   BioCyc; ASP404589:G1G9J-210-MONOMER; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000006382; Chromosome.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-UniRule.
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; -; 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; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A7H6S8.
DR   SWISS-2DPAGE; A7H6S8.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; FAD;
KW   Flavoprotein; FMN; Lyase; NADP; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Chorismate synthase"
FT                   /id="PRO_1000071966"
FT   NP_BIND         127..129
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   NP_BIND         247..248
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   NP_BIND         306..310
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         41
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         47
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         291
FT                   /note="FMN; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
FT   BINDING         332
FT                   /note="FMN"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00300"
SQ   SEQUENCE   381 AA;  40599 MW;  F41B5B7FDA59DCC3 CRC64;
     MTIRYLTAGE SHGPGLVAIA EGFPAGLAVD FDEVNRDLRR RQKGYGRGGR QKIEKDEAEF
     LAGLRGGVTL GAPIALVVWN KDHESWKDLV SPYARGGRPF TQVRPGHADL AGALKYALTD
     ARDVLERASA RSTAVTVALG SLAKQLLARF GVRVSSRVVA IGPRLRHVEE PPTDAERDAI
     EASDLHVEDE AVAAEWRALI DAEKARGGSI GGAFDVHATG LPIGLGSHVH PDRRLDARLA
     GALCGVQAIR AAEIGDGTQV GRSGPEFHDA IQHDPARGFH RPSNRAGGLE GGMTDGMPLR
     VRAYMKPIPT MLTPLATVDL ATREATQARY ERSDVCAVPA AAIVGEAVVA WELANAFLEK
     FGGDALVDVE KAVEAYAARI R
//

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