ID M4ZT66_9FLAO Unreviewed; 416 AA.
AC M4ZT66;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|ARBA:ARBA00012450};
DE EC=2.5.1.19 {ECO:0000256|ARBA:ARBA00012450};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000256|ARBA:ARBA00030046};
GN Name=aroA {ECO:0000313|EMBL:BAM99533.1};
GN ORFNames=BPAA_238 {ECO:0000313|EMBL:BAM99533.1};
OS Blattabacterium cuenoti BPAA.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1229512 {ECO:0000313|EMBL:BAM99533.1, ECO:0000313|Proteomes:UP000011815};
RN [1] {ECO:0000313|EMBL:BAM99533.1, ECO:0000313|Proteomes:UP000011815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPAA {ECO:0000313|EMBL:BAM99533.1,
RC ECO:0000313|Proteomes:UP000011815};
RX PubMed=23515978; DOI=10.1098/rsbl.2012.1153;
RA Tokuda G., Elbourne L.D.H., Kinjo Y., Saitoh S., Sabree Z., Hojo M.,
RA Yamada A., Hayashi Y., Shigenobu S., Bandi C., Paulsen I.T., Watanabe H.,
RA Lo N.;
RT "Maintenance of essential amino acid synthesis pathways in the
RT Blattabacterium cuenoti symbiont of a wood-feeding cockroach.";
RL Biol. Lett. 9:20121153-20121153(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-
CC carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702,
CC ChEBI:CHEBI:145989; EC=2.5.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00001901};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000256|ARBA:ARBA00004811}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family.
CC {ECO:0000256|ARBA:ARBA00009948}.
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DR EMBL; AP012548; BAM99533.1; -; Genomic_DNA.
DR RefSeq; WP_015429852.1; NC_020510.1.
DR AlphaFoldDB; M4ZT66; -.
DR STRING; 1229512.BPAA_238; -.
DR KEGG; blp:BPAA_238; -.
DR PATRIC; fig|1229512.3.peg.234; -.
DR eggNOG; COG0128; Bacteria.
DR HOGENOM; CLU_024321_0_0_10; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000011815; Chromosome.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IEA:UniProtKB-EC.
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-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.65.10.10; Enolpyruvate transferase domain; 3.
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 PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF5; PENTAFUNCTIONAL AROM POLYPEPTIDE; 1.
DR Pfam; PF00275; EPSP_synthase; 1.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 59..405
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
SQ SEQUENCE 416 AA; 47541 MW; F3A61368E870AECB CRC64;
MSSYIKIYKN RRGLYGSISI TGSKSISNRL LILKAIYKDD IHIENLSNCE DTKILKKSLI
SSSNILDIHH AGTAMRFLTS YFSIQEGKTV ILTGSDRMKE RPIFVLVEAL KKLGSEIHYL
EKEGFPPIQI FGKKILGGEI DMNAKISSQY ISSLMLIASQ FQMGLKIYLK GNITSIPYIK
MTFNLLTLAG IKADWKEKMI HIYPVKNQGK KCFSVESDWS SASYYYSMSA IAKKSHIILR
SYSNKSLQGD KKVCDIYNQY FGISTVFDQN VITLKKKLNF LLPRFIELDL NNTPDLAQTI
VVTCAAIGIK CSLKGLETLK IKETDRLKAL KEELLKFGVI TKITKSCLKI TDFYRKKIDS
FIRIRTYQDH RMAMSFSTFG LCSDFIKIEN PNVVEKSYPN FWKDLESLGF LIDYEE
//
