(data stored in ACNUC7421 zone)

SWISSPROT: A4ATP4_MARSH

ID   A4ATP4_MARSH            Unreviewed;       409 AA.
AC   A4ATP4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            EC=2.5.1.19 {ECO:0000256|HAMAP-Rule:MF_00210};
DE   AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSP synthase {ECO:0000256|HAMAP-Rule:MF_00210};
DE            Short=EPSPS {ECO:0000256|HAMAP-Rule:MF_00210};
GN   Name=aroA {ECO:0000256|HAMAP-Rule:MF_00210};
GN   OrderedLocusNames=FB2170_17056 {ECO:0000313|EMBL:EAR00814.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00814.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00814.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS00240586}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC         carboxyvinyl)-3-phosphoshikimate + phosphate;
CC         Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00210,
CC         ECO:0000256|SAAS:SAAS01118199};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 6/7. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS01089941}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
CC       ECO:0000256|SAAS:SAAS01089951}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00210, ECO:0000256|SAAS:SAAS00567303}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00210}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002157; EAR00814.1; -; Genomic_DNA.
DR   RefSeq; WP_013304617.1; NC_014472.1.
DR   STRING; 313603.FB2170_17056; -.
DR   EnsemblBacteria; EAR00814; EAR00814; FB2170_17056.
DR   KEGG; fbc:FB2170_17056; -.
DR   eggNOG; ENOG4107S18; Bacteria.
DR   eggNOG; COG0128; LUCA.
DR   HOGENOM; HOG000247372; -.
DR   KO; K00800; -.
DR   OMA; GEPRMEE; -.
DR   OrthoDB; 533829at2; -.
DR   BioCyc; MSP313603:G1GNS-188-MONOMER; -.
DR   UniPathway; UPA00053; UER00089.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase 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; 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; IPR036968; Enolpyruvate_Tfrase_sf.
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; 2.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATP4.
DR   SWISS-2DPAGE; A4ATP4.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00423060};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00215611};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS01089931};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00210,
KW   ECO:0000256|SAAS:SAAS00215594, ECO:0000313|EMBL:EAR00814.1}.
FT   DOMAIN       63    399       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       23     24       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   REGION      145    147       Shikimate-3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   ACT_SITE    292    292       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   ACT_SITE    320    320       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00210}.
FT   BINDING      28     28       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING      99     99       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     173    173       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     319    319       Shikimate-3-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00210}.
FT   BINDING     323    323       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     366    366       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
FT   BINDING     390    390       Phosphoenolpyruvate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00210}.
SQ   SEQUENCE   409 AA;  44635 MW;  B6F05B7EA0F46842 CRC64;
     MKLNLSGPAS DFLNSSVQIT GSKSESNRSL LLQALYPNIS IENLSNSDDA EVMQKGLAIS
     NGEVDIHHAG TAMRFLTGYF ASQPDKEVVL TGSQRMTERP VKVLVDALKN LGADIEYVNN
     EGYPPIKIKG KKIQKHQVSL PANISSQYIS SLLLIAPSLE NGLELNLVGE ITSVPYIKMT
     LGLLNQIGVE TSFSDNIIKV LPKNNVGRTE LVVESDWSSA SYFYSIVALS KVGSEIKLGS
     YKRDSLQGDS VLANIYESFG VDTTFVNNEI VLTKTQDCSL DLIECDLANA PDIAQTIAVT
     CLGLGIGCEL RGLHTLKIKE TDRLVAMHDE LTKFGADVVV TNETLTLKKS NSIKSGVSVD
     TYNDHRMAMA FGPLALKTSF NINDAEVVSK SYPDFWKDLE TLGFKLRKL
//

If you have problems or comments...

PBIL Back to PBIL home page