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 27-MAR-2024, entry version 139. 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; Actinomycetota; Actinomycetes; Mycobacteriales; 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.m111.011445; 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}. 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; 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; 83332-Rv2178c; -. DR DNASU; 888309; -. DR GeneID; 888309; -. DR KEGG; mtu:Rv2178c; -. DR TubercuList; Rv2178c; -. DR eggNOG; COG3200; Bacteria. DR InParanoid; O53512; -. DR OrthoDB; 9766852at2; -. 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: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 GO; GO:0051260; P:protein homooligomerization; IPI:MTBBASE. DR Gene3D; 3.20.20.70; Aldolase class I; 2. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002480; DAHP_synth_2. DR NCBIfam; TIGR01358; DAHP_synth_II; 1. DR PANTHER; PTHR21337:SF0; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1. DR PANTHER; PTHR21337; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE 1, 2; 1. DR Pfam; PF01474; DAHP_synth_2; 1. DR SUPFAM; SSF51569; Aldolase; 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 //