Phospho-2-dehydro-3-deoxyheptonate aldolase AroG

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O53512 (AROG_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › 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: K_M=25 µM for D-erythrose 4-phosphate (E4P) Ref.2 K_M=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: InterPro chorismate biosynthetic process Traceable author statement. Source: Reactome growth Inferred from mutant phenotype. Source: MTBBASE protein homooligomerization Inferred from physical interaction. Source: MTBBASE
Cellular component	cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	3-deoxy-7-phosphoheptulonate synthase activity Inferred from direct assay Ref.2. Source: MTBBASE manganese ion binding Inferred from direct assay Ref.2. Source: MTBBASE protein binding Inferred from physical interaction. 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

Substrate binding

Sites

Metal binding

Divalent cations

Metal binding

369

Divalent cations

Metal binding

411

Divalent cations

Metal binding

441

Divalent cations

Binding site

126

Susbtrate

Binding site

306

Susbtrate

Binding site

337

Susbtrate

Sequences

Sequence

Length

Mass (Da)

Tools

O53512 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 1BE844FAEF21C4C5
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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

« Hide

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. Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [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: 16288916] [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: 19556970] [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.

PIR

D70936.

RefSeq

NP_216694.1. NC_000962.2.

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	[»]
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	[»]

ProteinModelPortal

O53512.

SMR

O53512. Positions 1-462.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000000812; EBMYCP00000000812; EBMYCG00000000812.

GeneID

888309.

GenomeReviews

Gene locus Rv2178c in contig AL123456_GR.

KEGG

mtu:Rv2178c.

PATRIC

18153402. VBIMycTub87468_2429.

Organism-specific databases

TubercuList

Rv2178c.

Phylogenomic databases

GeneTree

EBGT00050000017425.

HOGENOM

HBG292577.

OMA

MAIVMTF.

ProtClustDB

CLSK863098.

Enzyme and pathway databases

Reactome

REACT_27295. Mycobacterium tuberculosis biological processes.

Family and domain databases

InterPro

IPR002480. DAHP_synth_2.
[Graphical view]

K01626.

PANTHER

PTHR21337. DAHP_synth_2. 1 hit.

Pfam

PF01474. DAHP_synth_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01358. DAHP_synth_II. 1 hit.

ProtoNet

Search...

Entry information

Entry name

AROG_MYCTU

Accession

Primary (citable) accession number: O53512

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents