ID A4YHV9_METS5 Unreviewed; 391 AA.
AC A4YHV9;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000256|ARBA:ARBA00012450};
DE EC=2.5.1.19 {ECO:0000256|ARBA:ARBA00012450};
GN OrderedLocusNames=Msed_1871 {ECO:0000313|EMBL:ABP96011.1};
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP96011.1, ECO:0000313|Proteomes:UP000000242};
RN [1] {ECO:0000313|EMBL:ABP96011.1, ECO:0000313|Proteomes:UP000000242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC {ECO:0000313|Proteomes:UP000000242};
RX PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP96011.1; -; Genomic_DNA.
DR AlphaFoldDB; A4YHV9; -.
DR STRING; 399549.Msed_1871; -.
DR KEGG; mse:Msed_1871; -.
DR eggNOG; arCOG04134; Archaea.
DR HOGENOM; CLU_024321_0_0_2; -.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000000242; 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; 2.
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; 2.
DR PIRSF; PIRSF000505; EPSPS; 1.
DR SUPFAM; SSF55205; EPT/RTPC-like; 1.
DR PROSITE; PS00104; EPSP_SYNTHASE_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABP96011.1}.
FT DOMAIN 7..57
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
FT DOMAIN 59..380
FT /note="Enolpyruvate transferase"
FT /evidence="ECO:0000259|Pfam:PF00275"
SQ SEQUENCE 391 AA; 42379 MW; 6544B8A32ABC3697 CRC64;
MFVEIEPSRI KGRVKAPPSK SLGIRYVFLS LLTEVSLENL PESDDVRVAI NAVKSLKEGK
DELYLGGSAT TLRMIIPVIL AMGRRVKLDG DDTLRRRPLN ALRWLPGKFS SNSLPMTVEG
SLGPETQIEG WESSQYISGL IYAYCLRGEG RIRVIPPISS RGYIFMTADV ISSIGGKVTI
QGEEITVECR NLRKFGGSVP GDYALASFYA VGAVLTGGEV EITNLYAPPS YVGDHDVVRM
VKEAGAESYV SENRWIVRDT GVRVPISVSI NDVPDLAPSL AALMAVIPGE SRIMDSERLR
IKESDRISTI LNTLASFGIS GSYSAGTITV KGGEPRRGEV ECPKDHRIAM MAGDLALRVG
GKITSAECVN KSNPGYWSDL SALGGKIRIH E
//
