AROG_MYCTU
ID AROG_MYCTU Reviewed; 462 AA.
AC O53512; L0T926;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase AroG;
DE EC=2.5.1.54 {ECO:0000269|PubMed:16288916};
DE AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE AltName: Full=DAHP synthase;
DE AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN Name=aroG; OrderedLocusNames=Rv2178c;
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 [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 [2]
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 [3] {ECO:0007744|PDB:2B7O}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH PHOSPHOENOLPYRUVATE
RP AND MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16288916; DOI=10.1016/j.jmb.2005.09.093;
RA Webby C.J., Baker H.M., Lott J.S., Baker E.N., Parker E.J.;
RT "The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from
RT Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry
RT for type I and type II enzymes.";
RL J. Mol. Biol. 354:927-939(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19556970; DOI=10.1038/emboj.2009.165;
RA Sasso S., Okvist M., Roderer K., Gamper M., Codoni G., Krengel U., Kast P.;
RT "Structure and function of a complex between chorismate mutase and DAHP
RT synthase: efficiency boost for the junior partner.";
RL EMBO J. 28:2128-2142(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA Webby C.J., Jiao W., Hutton R.D., Baker H.M., Baker E.N., Jameson G.B.,
RA Parker E.J.;
RT "Synergistic inhibition of the first enzyme of the shikimate pathway by
RT combinations of aromatic amino acids.";
RL Submitted (OCT-2009) to the PDB data bank.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
RA Webby C.J., Jiao W., Hutton R.D., Baker H.M., Baker E.N., Jameson G.B.,
RA Parker E.J.;
RT "Synergistic allostery of the first enzyme of the shikimate pathway reveals
RT a sophisticated regulatory network for the control of a branched
RT biosynthetic pathway.";
RL Submitted (JUL-2010) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RA Reichau S., Jiao W., Walker S.R., Hutton R.D., Parker E.J.;
RT "Potent inhibitors of a shikimate pathway enzyme from mycobacterium
RT tuberculosis combining mechanism- and modeling based design.";
RL Submitted (OCT-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes an aldol-like condensation reaction between
CC phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate
CC 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic
CC phosphate. {ECO:0000269|PubMed:16288916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000269|PubMed:16288916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14718;
CC Evidence={ECO:0000305|PubMed:16288916};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16288916};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16288916};
CC Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC Evidence={ECO:0000269|PubMed:16288916};
CC Note=Binds 1 divalent cation per subunit. The enzyme is active with
CC manganese, cobalt or cadmium ions. {ECO:0000269|PubMed:16288916};
CC -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan, tyrosine,
CC phenylalanine and chorismate. {ECO:0000269|PubMed:16288916}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for D-erythrose 4-phosphate (E4P)
CC {ECO:0000269|PubMed:16288916};
CC KM=37 uM for phosphoenolpyruvate (PEP) {ECO:0000269|PubMed:16288916};
CC Note=kcat is 3.1 sec(-1). {ECO:0000269|PubMed:16288916};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 1/7. {ECO:0000305|PubMed:16288916}.
CC -!- SUBUNIT: Homodimer. Interacts with Rv0948c.
CC {ECO:0000269|PubMed:16288916}.
CC -!- INTERACTION:
CC O53512; P9WIC1: Rv0948c; NbExp=2; IntAct=EBI-5241825, EBI-5241850;
CC -!- MASS SPECTROMETRY: Mass=51827; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:19556970};
CC -!- SIMILARITY: Belongs to the class-II DAHP synthase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44955.1; -; Genomic_DNA.
DR PIR; D70936; D70936.
DR RefSeq; NP_216694.1; NC_000962.3.
DR RefSeq; WP_003911784.1; NZ_NVQJ01000008.1.
DR PDB; 2B7O; X-ray; 2.30 A; A/B=1-462.
DR PDB; 2W19; X-ray; 2.15 A; A/B=1-462.
DR PDB; 2W1A; X-ray; 2.35 A; A/B=1-462.
DR PDB; 2YPO; X-ray; 2.00 A; A/B=1-462.
DR PDB; 2YPP; X-ray; 2.30 A; A/B=1-462.
DR PDB; 2YPQ; X-ray; 2.76 A; A/B=1-462.
DR PDB; 3KGF; X-ray; 2.00 A; A/B=1-462.
DR PDB; 3NUD; X-ray; 3.00 A; A/B=1-462.
DR PDB; 3NUE; X-ray; 2.50 A; A/B=1-462.
DR PDB; 3NV8; X-ray; 2.25 A; A/B=1-462.
DR PDB; 3PFP; X-ray; 2.35 A; A/B=1-462.
DR PDB; 3RZI; X-ray; 1.95 A; A/B=1-462.
DR PDB; 5CKV; X-ray; 2.79 A; A/B=1-462.
DR PDB; 5CKX; X-ray; 2.70 A; A/B=1-462.
DR PDB; 5E2L; X-ray; 2.50 A; A/B=1-462.
DR PDB; 5E40; X-ray; 2.05 A; A/B=1-462.
DR PDB; 5E4N; X-ray; 2.05 A; A/B=1-462.
DR PDB; 5E5G; X-ray; 1.95 A; A/B=1-462.
DR PDB; 5E7Z; X-ray; 2.40 A; A/B=1-462.
DR PDB; 5EX4; X-ray; 2.25 A; A/B=1-462.
DR PDB; 6PBJ; X-ray; 1.90 A; A/B=1-462.
DR PDBsum; 2B7O; -.
DR PDBsum; 2W19; -.
DR PDBsum; 2W1A; -.
DR PDBsum; 2YPO; -.
DR PDBsum; 2YPP; -.
DR PDBsum; 2YPQ; -.
DR PDBsum; 3KGF; -.
DR PDBsum; 3NUD; -.
DR PDBsum; 3NUE; -.
DR PDBsum; 3NV8; -.
DR PDBsum; 3PFP; -.
DR PDBsum; 3RZI; -.
DR PDBsum; 5CKV; -.
DR PDBsum; 5CKX; -.
DR PDBsum; 5E2L; -.
DR PDBsum; 5E40; -.
DR PDBsum; 5E4N; -.
DR PDBsum; 5E5G; -.
DR PDBsum; 5E7Z; -.
DR PDBsum; 5EX4; -.
DR PDBsum; 6PBJ; -.
DR AlphaFoldDB; O53512; -.
DR SMR; O53512; -.
DR IntAct; O53512; 1.
DR MINT; O53512; -.
DR STRING; 83332.Rv2178c; -.
DR PaxDb; O53512; -.
DR DNASU; 888309; -.
DR GeneID; 888309; -.
DR KEGG; mtu:Rv2178c; -.
DR TubercuList; Rv2178c; -.
DR eggNOG; COG3200; Bacteria.
DR InParanoid; O53512; -.
DR OMA; KVMMQMA; -.
DR PhylomeDB; O53512; -.
DR BRENDA; 2.5.1.54; 3445.
DR Reactome; R-MTU-964903; Chorismate via Shikimate Pathway.
DR SABIO-RK; O53512; -.
DR UniPathway; UPA00053; UER00084.
DR EvolutionaryTrace; O53512; -.
DR PRO; PR:O53512; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
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 GO; GO:0051260; P:protein homooligomerization; IPI:MTBBASE.
DR Gene3D; 3.20.20.70; -; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002480; DAHP_synth_2.
DR PANTHER; PTHR21337; PTHR21337; 1.
DR Pfam; PF01474; DAHP_synth_2; 1.
DR TIGRFAMs; TIGR01358; DAHP_synth_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Cadmium; Cobalt; Manganese; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..462
FT /note="Phospho-2-dehydro-3-deoxyheptonate aldolase AroG"
FT /id="PRO_0000414909"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 126
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 283..284
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 306
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 337
FT /ligand="phosphoenolpyruvate"
FT /ligand_id="ChEBI:CHEBI:58702"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 369
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 411
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT BINDING 441
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:16288916,
FT ECO:0007744|PDB:2B7O"
FT TURN 1..3
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2YPO"
FT HELIX 96..117
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6PBJ"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 167..187
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3NUE"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 215..230
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3RZI"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6PBJ"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:6PBJ"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:6PBJ"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3NUD"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:3RZI"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:3RZI"
FT HELIX 384..401
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:6PBJ"
FT STRAND 420..422
FT /evidence="ECO:0007829|PDB:6PBJ"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:3RZI"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6PBJ"
FT HELIX 446..461
FT /evidence="ECO:0007829|PDB:6PBJ"
SQ SEQUENCE 462 AA; 50641 MW; 1BE844FAEF21C4C5 CRC64;
MNWTVDIPID QLPSLPPLPT DLRTRLDAAL AKPAAQQPTW PADQALAMRT VLESVPPVTV
PSEIVRLQEQ LAQVAKGEAF LLQGGDCAET FMDNTEPHIR GNVRALLQMA VVLTYGASMP
VVKVARIAGQ YAKPRSADID ALGLRSYRGD MINGFAPDAA AREHDPSRLV RAYANASAAM
NLVRALTSSG LASLHLVHDW NREFVRTSPA GARYEALATE IDRGLRFMSA CGVADRNLQT
AEIYASHEAL VLDYERAMLR LSDGDDGEPQ LFDLSAHTVW IGERTRQIDG AHIAFAQVIA
NPVGVKLGPN MTPELAVEYV ERLDPHNKPG RLTLVSRMGN HKVRDLLPPI VEKVQATGHQ
VIWQCDPMHG NTHESSTGFK TRHFDRIVDE VQGFFEVHRA LGTHPGGIHV EITGENVTEC
LGGAQDISET DLAGRYETAC DPRLNTQQSL ELAFLVAEML RD
