(data stored in SCRATCH zone)

SWISSPROT: D4YXC5_SPHJU

ID   D4YXC5_SPHJU            Unreviewed;       358 AA.
AC   D4YXC5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 56.
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   ECO:0000313|EMBL:BAI95007.1};
GN   OrderedLocusNames=SJA_C1-01730 {ECO:0000313|EMBL:BAI95007.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95007.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95007.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:
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; 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}.
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DR   EMBL; AP010803; BAI95007.1; -; Genomic_DNA.
DR   RefSeq; WP_013038819.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-01730; -.
DR   EnsemblBacteria; BAI95007; BAI95007; SJA_C1-01730.
DR   GeneID; 29271879; -.
DR   KEGG; sjp:SJA_C1-01730; -.
DR   eggNOG; ENOG4105D10; Bacteria.
DR   eggNOG; COG0082; LUCA.
DR   HOGENOM; HOG000060335; -.
DR   KO; K01736; -.
DR   OMA; MLSINAV; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000007753; Chromosome 1.
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; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR   PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXC5.
DR   SWISS-2DPAGE; D4YXC5.
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:UP000007753};
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, ECO:0000256|RuleBase:RU000605,
KW   ECO:0000313|EMBL:BAI95007.1}; NADP {ECO:0000256|HAMAP-Rule:MF_00300};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   NP_BIND     125    127       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     237    238       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   NP_BIND     297    301       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING      48     48       NADP. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING      54     54       NADP. {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING     282    282       FMN; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00300}.
FT   BINDING     323    323       FMN. {ECO:0000256|HAMAP-Rule:MF_00300}.
SQ   SEQUENCE   358 AA;  38219 MW;  C20FB57E05D6D901 CRC64;
     MSFNTFGRVF RFSTWGESHG PAIGAMVDGC PPGLPLTEAD IQPFLDKRKP GTSKFTTRRR
     EADEVRILSG VFEGRTTGTP ISLMIENTDQ RSKDYSEVAK AYRPGHADYA YDAKYGFRDY
     RGGGRSSARE TASRVAAGAV ARLVIPDVDI FAYVTEIGGD AIDPARFDAS EIDNNPFFCP
     DRQAAKRWEK LVDDARKDGS SLGAVVECIA SGVPAGWGAP LYAKLDSELA AAMMSINAVK
     GVEIGDGFAA ARLRGEQNAD PMRPGNEGNP VFLANHAGGI AGGISTGQPV KVRIAFKPTS
     SILIPVETVT REGEASDIVT KGRHDPCVGI RGVPVVEAMM ALVLADQKLL HRAQCGEG
//

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