Skip Header

Contribute Send feedback
Read comments (?) or add your own

A2VJL9 (A2VJL9_MYCTU) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
ATP phosphoribosyltransferase HAMAP MF_00079

Short name=ATP-PRT HAMAP MF_00079
Short name=ATP-PRTase HAMAP MF_00079
EC=2.4.2.17 HAMAP MF_00079
Gene names
Name:hisG HAMAP MF_00079
ORF Names:TBCG_02069 EMBL EAY60350.1
OrganismMycobacterium tuberculosis C EMBL EAY60350.1
Taxonomic identifier348776 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of hisG enzymatic activity By similarity. HAMAP MF_00079

Catalytic activity

1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00079 SAAS SAAS013820

Cofactor

Magnesium By similarity. HAMAP MF_00079

Enzyme regulation

Feedback inhibited by histidine By similarity. HAMAP MF_00079

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_00079 SAAS SAAS013820

Subunit structure

Equilibrium between an active dimeric form, an inactive hexameric form and higher aggregates. Interconversion between the various forms is largely reversible and is influenced by the natural substrates and inhibitors of the enzyme By similarity. HAMAP MF_00079

Subcellular location

Cytoplasm By similarity HAMAP MF_00079.

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily. HAMAP MF_00079

Sequences

Sequence LengthMass (Da)Tools
A2VJL9 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: C248C57399302B2A

FASTA28430,481
        10         20         30         40         50         60 
MLRVAVPNKG ALSEPATEIL AEAGYRRRTD SKDLTVIDPV NNVEFFFLRP KDIAIYVGSG 

        70         80         90        100        110        120 
ELDFGITGRD LVCDSGAQVR ERLALGFGSS SFRYAAPAGR NWTTADLAGM RIATAYPNLV 

       130        140        150        160        170        180 
RKDLATKGIE ATVIRLDGAV EISVQLGVAD AIADVVGSGR TLSQHDLVAF GEPLCDSEAV 

       190        200        210        220        230        240 
LIERAGTDGQ DQTEARDQLV ARVQGVVFGQ QYLMLDYDCP RSALKKATAI TPGLESPTIA 

       250        260        270        280 
PLADPDWVAI RALVPRRDVN GIMDELAAIG AKAILASDIR FCRF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH482373 Genomic DNA. Translation: EAY60350.1.

3D structure databases

ProteinModelPortalA2VJL9.
SMRA2VJL9. Positions 1-284.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC26048384. VBIMycTub57268_2242.

Phylogenomic databases

OMAIMLHAPS.

Family and domain databases

HAMAPMF_00079. HisG_Long.
[Tree]
InterProIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR020621. ATP_PRibTrfase_HisG_long.
IPR013115. HisG_C.
IPR011322. N-reg_PII-like_a/b.
IPR015867. N-reg_PII/ATP_PRibTrfase_C.
[Graphical view]
Gene3DG3DSA:3.30.70.120. PII_glnB. 1 hit.
PANTHERPTHR21403. ATP_phspho_trans. 1 hit.
PfamPF01634. HisG. 1 hit.
PF08029. HisG_C. 1 hit.
[Graphical view]
SUPFAMSSF54913. N-reg_PII-like_a/b. 1 hit.
TIGRFAMsTIGR00070. HisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA2VJL9_MYCTU
AccessionPrimary (citable) accession number: A2VJL9
Entry history
Integrated into UniProtKB/TrEMBL: March 20, 2007
Last sequence update: March 20, 2007
Last modified: December 14, 2011
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)