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P60759 (HIS1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP phosphoribosyltransferase
Short name=ATP-PRT
Short name=ATP-PRTase
EC=2.4.2.17
Gene names
Name:hisG
Ordered Locus Names:Rv2121c, MT2181
ORF Names:MTCY261.17c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium 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-Rule MF_00079

Catalytic activity

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

Cofactor

Magnesium.

Enzyme regulation

Feedback inhibited by histidine. Also inhibited by AMP. HAMAP-Rule MF_00079

Pathway

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

Subcellular location

Cytoplasm By similarity.

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-Rule MF_00079
PRO_0000151857

Secondary structure

1 ...................................................... 284
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60759 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
AL123456 Genomic DNA. Translation: CCP44896.1.
PIRD70513.
RefSeqNP_216637.1. NC_000962.3.
NP_336650.1. NC_002755.2.
YP_006515537.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NH7X-ray2.70A1-284[»]
1NH8X-ray1.80A1-284[»]
ProteinModelPortalP60759.
SMRP60759. Positions 1-284.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2121c.

Proteomic databases

PRIDEP60759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK46464; AAK46464; MT2181.
GeneID13316928.
888689.
924287.
KEGGmtc:MT2181.
mtu:Rv2121c.
mtv:RVBD_2121c.
PATRIC18126552. VBIMycTub22151_2389.

Organism-specific databases

TubercuListRv2121c.

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223250.
KOK00765.
OMAVATEFPN.
ProtClustDBPRK00489.

Enzyme and pathway databases

UniPathwayUPA00031; UER00006.

Family and domain databases

Gene3D3.30.70.120. 1 hit.
HAMAPMF_00079. HisG_Long.
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]
PANTHERPTHR21403. PTHR21403. 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...

Other

BindingDBP60759.
ChEMBLCHEMBL6086.
DrugBankDB00131. Adenosine monophosphate.
EvolutionaryTraceP60759.

Entry information

Entry nameHIS1_MYCTU
AccessionPrimary (citable) accession number: P60759
Secondary accession number(s): L0TBL0, O33256
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents