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A4YI31 (HIS1_METS5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:Msed_1943
OrganismMetallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]
Taxonomic identifier399549 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera

Protein attributes

Sequence length285 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-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 By similarity.

Enzyme regulation

Feedback inhibited by histidine By similarity. 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

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 – 285285ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_1000071207

Sequences

Sequence LengthMass (Da)Tools
A4YI31 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: AD03A0A6731DE60F

FASTA28530,922
        10         20         30         40         50         60 
MKIAIPNKGR LQGPALQFLN SVGIKPMAND DRALMVPTSW EGVQLVTIRT EDIPNIVETG 

        70         80         90        100        110        120 
AVDLGITGLD YVMESGADVE ELVKLDFGKS RLVLAVPMSW NIEDPRDMPK NVRIATKYHN 

       130        140        150        160        170        180 
IARAYLERKG IEARLVKISG AAEIMPSLGA ADAIIDVTST GTTLKLHGLK PIDVVSESYA 

       190        200        210        220        230        240 
MVIGNKNWMK SEEADRINLV LTMMKGALSA RGKKMIFMNV DDVNLEAVVS SLPAMLAPAV 

       250        260        270        280 
SKLSNSNAWE VVTVTDEEML PEVIAKAKTA GARDIVVVNI EKVIK 

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References

[1]"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51363 / DSM 5348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000682 Genomic DNA. Translation: ABP96083.1.
RefSeqYP_001192007.1. NC_009440.1.

3D structure databases

ProteinModelPortalA4YI31.
ModBaseSearch...

Protein-protein interaction databases

STRING399549.Msed_1943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP96083; ABP96083; Msed_1943.
GeneID5103330.
KEGGmse:Msed_1943.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223247.
KOK00765.
OMATIRTEDI.
ProtClustDBPRK00489.

Enzyme and pathway databases

BioCycMSED399549:GH1O-1988-MONOMER.
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...

Entry information

Entry nameHIS1_METS5
AccessionPrimary (citable) accession number: A4YI31
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2007
Last modified: May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families