AROA_MYCTU
ID AROA_MYCTU Reviewed; 450 AA.
AC P9WPY5; L0TDI9; P22487;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2123856};
DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:11483005};
DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2123856};
DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2123856};
DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2123856};
GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000303|PubMed:2123856};
GN OrderedLocusNames=Rv3227;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=2123856; DOI=10.1128/jb.172.12.6774-6782.1990;
RA Garbe T., Jones C., Charles I.G., Dougan G., Young D.;
RT "Cloning and characterization of the aroA gene from Mycobacterium
RT tuberculosis.";
RL J. Bacteriol. 172:6774-6782(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=11483005; DOI=10.1006/prep.2001.1457;
RA Oliveira J.S., Pinto C.A., Basso L.A., Santos D.S.;
RT "Cloning and overexpression in soluble form of functional shikimate kinase
RT and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium
RT tuberculosis.";
RL Protein Expr. Purif. 22:430-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RA Bourenkov G.P., Kachalova G.S., Strizhov N., Bruning M., Vagin A.,
RA Bartunik H.D.;
RT "Mycobacterium tuberculosis EPSP synthase in unliganded state.";
RL Submitted (FEB-2005) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH
RP SHIKIMATE-3-PHOSPHATE AND PHOSPHOENOLPYRUVATE, AND ACTIVE SITE.
RA Kachalova G.S., Burenkov G.P., Strizhov N.I., Brunning M.G., Bartunik H.D.;
RT "Complex of 3-phosphoshikimate 1-carboxyvinyltransferase with S3P.";
RL Submitted (NOV-2006) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of
CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate
CC (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic
CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00210,
CC ECO:0000269|PubMed:11483005}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00210, ECO:0000269|PubMed:11483005};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 6/7. {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210,
CC ECO:0000269|PubMed:11483005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}.
CC -!- SIMILARITY: Belongs to the EPSP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00210, ECO:0000305}.
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DR EMBL; X52269; CAA36510.1; -; Genomic_DNA.
DR EMBL; M62708; AAA25356.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46046.1; -; Genomic_DNA.
DR PIR; E70590; E70590.
DR RefSeq; NP_217744.1; NC_000962.3.
DR RefSeq; WP_003416914.1; NZ_NVQJ01000003.1.
DR PDB; 2BJB; X-ray; 1.80 A; A=1-450.
DR PDB; 2O0B; X-ray; 1.15 A; A=1-450.
DR PDB; 2O0D; X-ray; 1.60 A; A=1-450.
DR PDB; 2O0E; X-ray; 1.81 A; A=1-450.
DR PDB; 2O0X; X-ray; 1.96 A; A=1-450.
DR PDB; 2O0Z; X-ray; 2.00 A; A=1-450.
DR PDB; 2O15; X-ray; 1.95 A; A=1-450.
DR PDBsum; 2BJB; -.
DR PDBsum; 2O0B; -.
DR PDBsum; 2O0D; -.
DR PDBsum; 2O0E; -.
DR PDBsum; 2O0X; -.
DR PDBsum; 2O0Z; -.
DR PDBsum; 2O15; -.
DR AlphaFoldDB; P9WPY5; -.
DR SMR; P9WPY5; -.
DR STRING; 83332.Rv3227; -.
DR PaxDb; P9WPY5; -.
DR DNASU; 888753; -.
DR GeneID; 888753; -.
DR KEGG; mtu:Rv3227; -.
DR TubercuList; Rv3227; -.
DR eggNOG; COG0128; Bacteria.
DR OMA; YEDHRMA; -.
DR PhylomeDB; P9WPY5; -.
DR BRENDA; 2.5.1.19; 3445.
DR Reactome; R-MTU-964903; Chorismate via Shikimate Pathway.
DR UniPathway; UPA00053; UER00089.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IDA:MTBBASE.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IDA:MTBBASE.
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; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..450
FT /note="3-phosphoshikimate 1-carboxyvinyltransferase"
FT /id="PRO_0000088273"
FT REGION 426..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210"
FT BINDING 23..24
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 28
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 94..97
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 124
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 167..169
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 196
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 336
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 340
FT /ligand="3-phosphoshikimate"
FT /ligand_id="ChEBI:CHEBI:145989"
FT /evidence="ECO:0000269|Ref.6"
FT BINDING 344
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 385
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT BINDING 410
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00210,
FT ECO:0000269|Ref.6"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2O0B"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:2BJB"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2O15"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2BJB"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2O0B"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:2O0B"
FT HELIX 415..423
FT /evidence="ECO:0007829|PDB:2O0B"
SQ SEQUENCE 450 AA; 46426 MW; 27BB86F9412A07D5 CRC64;
MKTWPAPTAP TPVRATVTVP GSKSQTNRAL VLAALAAAQG RGASTISGAL RSRDTELMLD
ALQTLGLRVD GVGSELTVSG RIEPGPGARV DCGLAGTVLR FVPPLAALGS VPVTFDGDQQ
ARGRPIAPLL DALRELGVAV DGTGLPFRVR GNGSLAGGTV AIDASASSQF VSGLLLSAAS
FTDGLTVQHT GSSLPSAPHI AMTAAMLRQA GVDIDDSTPN RWQVRPGPVA ARRWDIEPDL
TNAVAFLSAA VVSGGTVRIT GWPRVSVQPA DHILAILRQL NAVVIHADSS LEVRGPTGYD
GFDVDLRAVG ELTPSVAALA ALASPGSVSR LSGIAHLRGH ETDRLAALST EINRLGGTCR
ETPDGLVITA TPLRPGIWRA YADHRMAMAG AIIGLRVAGV EVDDIAATTK TLPEFPRLWA
EMVGPGQGWG YPQPRSGQRA RRATGQGSGG
