MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210}; EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210}; AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210}; Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210}; Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210}; |
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| MyHits synonyms | AROA_BURCC , B1JXR9 , 7C899B7683B15A65 |
 Legends: 1, ACT_SITE Proton acceptor. {ECO:0000255|HAMAP- Rule:MF_00210}; 2, ACT_SITE Proton donor. {ECO:0000255|HAMAP- Rule:MF_00210}; 3, BINDING Shikimate-3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}; 4, BINDING Phosphoenolpyruvate. {ECO:0000255|HAMAP- Rule:MF_00210}; 5, REGION Shikimate-3-phosphate binding. {ECO:0000255|HAMAP-Rule:MF_00210}; 6, REGION Phosphoenolpyruvate. {ECO:0000255|HAMAP- Rule:MF_00210}; 7, ipat:EPSP_SYNTHASE_2 [T]; 8, ipat:EPSP_SYNTHASE_1 [T].
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ID AROA_BURCC Reviewed; 434 AA.
AC B1JXR9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 30-NOV-2016, entry version 60.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210};
GN OrderedLocusNames=Bcenmc03_1004;
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-
RT 3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-
CC phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and
CC inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate =
CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.
CC {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC biosynthesis; chorismate from D-erythrose 4-phosphate and
CC phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00210}.
DR EMBL; CP000958; ACA90181.1; -; Genomic_DNA.
DR RefSeq; WP_012328122.1; NC_010508.1.
DR ProteinModelPortal; B1JXR9; -.
DR SMR; B1JXR9; -.
DR EnsemblBacteria; ACA90181; ACA90181; Bcenmc03_1004.
DR KEGG; bcm:Bcenmc03_1004; -.
DR PATRIC; 19089014; VBIBurCen61509_1034.
DR HOGENOM; HOG000247372; -.
DR KO; K00800; -.
DR OMA; ETDHRVA; -.
DR OrthoDB; POG091H02JK; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000002169; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01556; EPSP_synthase; 1.
DR Gene3D; 3.65.10.10; -; 2.
DR HAMAP; MF_00210; EPSP_synth; 1.
DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR InterPro; IPR006264; EPSP_synthase.
DR InterPro; IPR023193; EPSP_synthase_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR01356; aroA; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Complete proteome; Cytoplasm; Transferase.
FT CHAIN 1 434 3-phosphoshikimate 1-
FT carboxyvinyltransferase.
FT /FTId=PRO_1000099670.
FT REGION 22 23 Shikimate-3-phosphate binding.
FT {ECO:0000255|HAMAP-Rule:MF_00210}.
FT REGION 91 94 Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
FT REGION 168 170 Shikimate-3-phosphate binding.
FT {ECO:0000255|HAMAP-Rule:MF_00210}.
FT ACT_SITE 320 320 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
FT ACT_SITE 348 348 Proton donor. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
FT BINDING 27 27 Shikimate-3-phosphate.
FT {ECO:0000255|HAMAP-Rule:MF_00210}.
FT BINDING 121 121 Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
FT BINDING 199 199 Shikimate-3-phosphate.
FT {ECO:0000255|HAMAP-Rule:MF_00210}.
FT BINDING 347 347 Shikimate-3-phosphate.
FT {ECO:0000255|HAMAP-Rule:MF_00210}.
FT BINDING 351 351 Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
FT BINDING 394 394 Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
FT BINDING 419 419 Phosphoenolpyruvate. {ECO:0000255|HAMAP-
FT Rule:MF_00210}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 345 363 ipat:EPSP_SYNTHASE_2 [T]
FT MYHIT 11 427 ipfam:EPSP_synthase [T]
FT MYHIT 10 434 ihamap:EPSP_synth [T]
FT MYHIT 87 101 ipat:EPSP_SYNTHASE_1 [T]
SQ SEQUENCE 434 AA; 46320 MW; 7C899B7683B15A65 CRC64;
MDYLDLGPYS SASGTVRLPG SKSISNRVLL LAALAEGETT ITNLLDSDDT RVMLDALGKL
GVKLARDGDT CVVTGTRGAF TAKTADLFLG NAGTAVRPLT AALAVNGGDY RVHGVPRMHE
RPIGDLVDGL RQIGAQIDYE LNEGYPPLRI KPATISVDAP IRVRGDVSSQ FLTALLMTLP
LVKAKDGRTV VEVDGELISK PYIDITIRLM ARFGVTVERD GWQRFVVPAG VRYKSPGRIM
VEGDASSASY FLAAGALGGG PLRVEGVGRA SIQGDVGFAN ALMQMGANVT MGDDWIDVRG
IGHDHGKLEP IDMDFNLIPD AAMTIAVAAL FANGTSTLRN IASWRVKETD RIAAMATELR
KVGAIVEEGP DYLVVTPPEK LTPNAAIDTY DDHRMAMCFS LVSLGGVPVR INDPKCVGKT
FPDYFDRFAA LAKA
//
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