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Reviewed, UniProtKB/Swiss-Prot P60759 (HIS1_MYCTU)

Last modified February 9, 2010. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    ATP phosphoribosyltransferase
      Short name=ATP-PRTase
      Short name=ATP-PRT
    EC=2.4.2.17
Gene names
Name: hisG
Ordered Locus Names: Rv2121c, MT2181
ORF Names: MTCY261.17c
OrganismMycobacterium tuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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

Cofactor

Magnesium. HAMAP MF_00079

Enzyme regulation

Feedback inhibited by histidine. Also inhibited by AMP. 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

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. HAMAP MF_00079

Subcellular location

Cytoplasm By similarity HAMAP MF_00079.

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284ATP phosphoribosyltransferase HAMAP MF_00079
PRO_0000151857

Secondary structure

.................................................... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60759-1 [UniParc].

Last modified April 13, 2004. 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

References

« Hide '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. expand/collapse author list , 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: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis."
Cho Y., Sharma V., Sacchettini J.C.
J. Biol. Chem. 278:8333-8339(2003) [PubMed: 12511575] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH HISTIDINE AND AMP.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842578 Genomic DNA. Translation: CAB10710.1.
AE000516 Genomic DNA. Translation: AAK46464.1.
PIRD70513.
RefSeqNP_216637.1.
NP_336650.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NH7X-ray2.70A1-284[»]
1NH8X-ray1.80A1-284[»]
ModBaseSearch...

Genome annotation databases

GeneID888689.
924287.
GenomeReviewsGene locus MT2181 in contig AE000516_GR.
KEGGmtc:MT2181.
mtu:Rv2121c.
TIGRMT2181.

Organism-specific databases

TubercuListRv2121c.

Phylogenomic databases

HOGENOMHBG391868.
OMAYLRPRDI.

Enzyme and pathway databases

BRENDA2.4.2.17. 809.

Family and domain databases

HAMAPMF_00079. HisG_Long.
[Tree]
InterProIPR001348. ATP_PRibTrfase.
IPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR020621. ATP_PRibTrfase_subgr.
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]
TIGRFAMsTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00131. Adenosine monophosphate.

Entry information

Entry nameHIS1_MYCTU
AccessionPrimary (citable) accession number: P60759
Secondary accession number(s): O33256
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: February 9, 2010
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents