O53512 (AROG_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospho-2-dehydro-3-deoxyheptonate aldolase AroG
EC=2.5.1.54

Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthase
Phospho-2-keto-3-deoxyheptonate aldolase

Gene names

Name:	aroG
Ordered Locus Names:	Rv2178c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes an aldol-like condensation reaction between phosphoenolpyruvate (PEP) and D-erythrose 4-phosphate (E4P) to generate 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAH7P) and inorganic phosphate. Ref.2
Catalytic activity	Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.
Cofactor	Binds 2 divalent cations per subunit. The enzyme is active with manganese, cobalt or cadmium ions. Ref.2
Enzyme regulation	Feedback inhibited by tryptophan, tyrosine, phenylalanine and chorismate. Ref.2
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Subunit structure	Homodimer. Interacts with Rv0948c. Ref.2
Sequence similarities	Belongs to the class-II DAHP synthase family.
Biophysicochemical properties	Kinetic parameters: KM=25 µM for D-erythrose 4-phosphate (E4P) Ref.2 KM=37 µM for phosphoenolpyruvate (PEP)
Mass spectrometry	Molecular mass is 51827 Da from positions 1 - 462. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	Metal-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW chorismate biosynthetic process Traceable author statement. Source: Reactome growth Inferred from mutant phenotype PubMed 12657046. Source: MTBBASE protein homooligomerization Inferred from physical interaction PubMed 15721768. Source: MTBBASE
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay PubMed 14532352PubMed 15525680. Source: MTBBASE
Molecular_function	3-deoxy-7-phosphoheptulonate synthase activity Inferred from direct assay PubMed 15721768Ref.2. Source: MTBBASE manganese ion binding Inferred from direct assay Ref.2. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 462

462

Phospho-2-dehydro-3-deoxyheptonate aldolase AroG

PRO_0000414909

Regions

Region

283 – 284

2

Substrate binding

Sites

Metal binding

87

1

Divalent cations

Metal binding

369

1

Divalent cations

Metal binding

411

1

Divalent cations

Metal binding

441

1

Divalent cations

Binding site

126

1

Substrate

Binding site

306

1

Substrate

Binding site

337

1

Substrate

Secondary structure

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462

Helix Strand Turn

Details...

Turn

1 – 3

3

Beta strand

4 – 8

5

Helix

20 – 30

11

Helix

42 – 52

11

Helix

61 – 75

15

Beta strand

80 – 85

6

Helix

91 – 93

3

Helix

96 – 117

22

Beta strand

121 – 126

6

Beta strand

143 – 145

3

Turn

150 – 152

3

Beta strand

155 – 158

4

Helix

159 – 162

4

Helix

168 – 188

21

Turn

189 – 192

4

Helix

194 – 207

14

Beta strand

208 – 210

3

Helix

211 – 230

20

Helix

236 – 238

3

Beta strand

244 – 248

5

Helix

252 – 257

6

Beta strand

259 – 261

3

Beta strand

266 – 268

3

Beta strand

271 – 273

3

Beta strand

277 – 281

5

Turn

283 – 285

3

Helix

291 – 298

8

Beta strand

303 – 307

5

Helix

313 – 323

11

Beta strand

331 – 336

6

Turn

340 – 342

3

Helix

343 – 356

14

Beta strand

362 – 365

4

Turn

367 – 369

3

Beta strand

371 – 374

4

Beta strand

380 – 383

4

Helix

384 – 401

18

Beta strand

407 – 412

6

Beta strand

420 – 422

3

Turn

423 – 426

4

Helix

431 – 433

3

Beta strand

439 – 441

3

Helix

446 – 461

16

Sequences

	Sequence		Length	Mass (Da)
	O53512 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 1BE844FAEF21C4C5	FASTA	462	50,641
	10 20 30 40 50 60 MNWTVDIPID QLPSLPPLPT DLRTRLDAAL AKPAAQQPTW PADQALAMRT VLESVPPVTV 70 80 90 100 110 120 PSEIVRLQEQ LAQVAKGEAF LLQGGDCAET FMDNTEPHIR GNVRALLQMA VVLTYGASMP 130 140 150 160 170 180 VVKVARIAGQ YAKPRSADID ALGLRSYRGD MINGFAPDAA AREHDPSRLV RAYANASAAM 190 200 210 220 230 240 NLVRALTSSG LASLHLVHDW NREFVRTSPA GARYEALATE IDRGLRFMSA CGVADRNLQT 250 260 270 280 290 300 AEIYASHEAL VLDYERAMLR LSDGDDGEPQ LFDLSAHTVW IGERTRQIDG AHIAFAQVIA 310 320 330 340 350 360 NPVGVKLGPN MTPELAVEYV ERLDPHNKPG RLTLVSRMGN HKVRDLLPPI VEKVQATGHQ 370 380 390 400 410 420 VIWQCDPMHG NTHESSTGFK TRHFDRIVDE VQGFFEVHRA LGTHPGGIHV EITGENVTEC 430 440 450 460 LGGAQDISET DLAGRYETAC DPRLNTQQSL ELAFLVAEML RD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes." Webby C.J., Baker H.M., Lott J.S., Baker E.N., Parker E.J. J. Mol. Biol. 354:927-939(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS AND MANGANESE IONS, FUNCTION AS A DAHP SYNTHASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR, SUBUNIT. Strain: ATCC 25618 / H37Rv.
[3]	"Structure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partner." Sasso S., Okvist M., Roderer K., Gamper M., Codoni G., Krengel U., Kast P. EMBO J. 28:2128-2142(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.
[4]	"Synergistic inhibition of the first enzyme of the shikimate pathway by combinations of aromatic amino acids." Webby C.J., Jiao W., Hutton R.D., Baker H.M., Baker E.N., Jameson G.B., Parker E.J. Submitted (OCT-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
[5]	"Synergistic allostery of the first enzyme of the shikimate pathway reveals a sophisticated regulatory network for the control of a branched biosynthetic pathway." Webby C.J., Jiao W., Hutton R.D., Baker H.M., Baker E.N., Jameson G.B., Parker E.J. Submitted (JUL-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
[6]	"Potent inhibitors of a shikimate pathway enzyme from mycobacterium tuberculosis combining mechanism- and modeling based design." Reichau S., Jiao W., Walker S.R., Hutton R.D., Parker E.J. Submitted (OCT-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842579 Genomic DNA. Translation: CAA17482.1.
AL123456 Genomic DNA. Translation: CCP44955.1.

PIR

D70936.

RefSeq

NP_216694.1. NC_000962.3.
YP_006515597.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B7O	X-ray	2.30	A/B	1-462	[»]
2W19	X-ray	2.15	A/B	1-462	[»]
2W1A	X-ray	2.35	A/B	1-462	[»]
2YPO	X-ray	2.00	A/B	1-462	[»]
2YPP	X-ray	2.30	A/B	1-462	[»]
2YPQ	X-ray	2.76	A/B	1-462	[»]
3KGF	X-ray	2.00	A/B	1-462	[»]
3NUD	X-ray	3.00	A/B	1-462	[»]
3NUE	X-ray	2.50	A/B	1-462	[»]
3NV8	X-ray	2.25	A/B	1-462	[»]
3PFP	X-ray	2.35	A/B	1-462	[»]
3RZI	X-ray	1.95	A/B	1-462	[»]

ProteinModelPortal

O53512.

SMR

O53512. Positions 1-462.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7298545.

STRING

83332.Rv2178c.

Proteomic databases

PRIDE

O53512.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

13318866.
888309.

KEGG

mtu:Rv2178c.

PATRIC

18153402. VBIMycTub87468_2429.

Organism-specific databases

TubercuList

Rv2178c.

Phylogenomic databases

HOGENOM

HOG000242917.

KO

K01626.

OMA

HEALLLH.

ProtClustDB

CLSK863098.

Enzyme and pathway databases

Reactome

REACT_27295. Mycobacterium tuberculosis biological processes.

UniPathway

UPA00053; UER00084.

Family and domain databases

InterPro

IPR002480. DAHP_synth_2.
[Graphical view]

PANTHER

PTHR21337. PTHR21337. 1 hit.

Pfam

PF01474. DAHP_synth_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01358. DAHP_synth_II. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O53512.

Entry information

Entry name

AROG_MYCTU

Accession

Primary (citable) accession number: O53512
Secondary accession number(s): L0T926

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	June 1, 1998
Last modified:	May 29, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program