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Q8KB10 (HIS1_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. 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:CT1988
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length293 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-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00079

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00079

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 HAMAP-Rule MF_00079.

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Long subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP phosphoribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 293293ATP phosphoribosyltransferase HAMAP-Rule MF_00079
PRO_0000151843

Sequences

Sequence LengthMass (Da)Tools
Q8KB10 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 8E0EBA31FAB20ABE

FASTA29332,103
        10         20         30         40         50         60 
MSNNKVLKLG LPKGSLQDST LELFANAGFH FSVQSRSYFP SIDDDELEAI LIRAQEMGRY 

        70         80         90        100        110        120 
VSLGAFDAGL TGKDWIIETD ADVVEVADLV YSKASMRPVR WVLAVPESSP IKTVKDLEGK 

       130        140        150        160        170        180 
HIATEVVNIT KKYLAENGVN ASVEFSWGAT EVKPPELADA IVEVTETGSS LRANKLRIVE 

       190        200        210        220        230        240 
TVLQSNTQLI ANKAAWADPW KRKKIENMAM LLQGAINAQG KVGLKMNAPK AALDKIMSGI 

       250        260        270        280        290 
PALRQPTVSD LADKEWVALE VIVSEKIVRT LIPELKRAGA EGIFEYNINK LID 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM73206.1.
RefSeqNP_662864.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ8KB10.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT1988.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM73206; AAM73206; CT1988.
GeneID1007573.
KEGGcte:CT1988.
PATRIC21401795. VBIChlTep116050_1801.

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223250.
KOK00765.
OMAVMELGFG.
OrthoDBEOG66MQT3.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-2028-MONOMER.
UniPathwayUPA00031; UER00006.

Family and domain databases

Gene3D3.30.70.120. 1 hit.
HAMAPMF_00079. HisG_Long.
InterProIPR013820. ATP_PRibTrfase_cat.
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. SSF54913. 1 hit.
TIGRFAMsTIGR00070. hisG. 1 hit.
TIGR03455. HisG_C-term. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS1_CHLTE
AccessionPrimary (citable) accession number: Q8KB10
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 1, 2002
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways