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A9KNX6 (HIS1_CLOPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:Cphy_2786
OrganismClostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]
Taxonomic identifier357809 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length215 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_01018

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01018

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP-Rule MF_01018

Subunit structure

Heteromultimer composed of HisG and HisZ subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01018.

Domain

Lacks the C-terminal regulatory region which is replaced by HisZ. HAMAP-Rule MF_01018

Sequence similarities

Belongs to the ATP phosphoribosyltransferase family. Short subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215ATP phosphoribosyltransferase HAMAP-Rule MF_01018
PRO_1000084156

Sequences

Sequence LengthMass (Da)Tools
A9KNX6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: DD8F972D5E54CF65

FASTA21524,091
        10         20         30         40         50         60 
MKYITIALAK GRLAKKALEI LEQIGITCDE MKDPTSRKLI FTNEELKLRF FLAKANDVPT 

        70         80         90        100        110        120 
YVEYGAADIG VVGKDTILEE GRKMYEVLDL NLGKCRMCIA GPASAKELLH HGELIRVATK 

       130        140        150        160        170        180 
YPNIAKDYFY NKKHQTVEII KLNGSIELAP IVGLSEVIVD IVETGSTLKE NGLEVLEEIC 

       190        200        210 
PLSARVVVNQ VSMKMEHERI TKMINDLREV LTEAQ 

« Hide

References

[1]"Complete genome sequence of Clostridium phytofermentans ISDg."
Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. expand/collapse author list , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000885 Genomic DNA. Translation: ABX43146.1.
RefSeqYP_001559885.1. NC_010001.1.

3D structure databases

ProteinModelPortalA9KNX6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357809.Cphy_2786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX43146; ABX43146; Cphy_2786.
GeneID5742101.
KEGGcpy:Cphy_2786.
PATRIC19505334. VBICloPhy16213_2903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0040.
HOGENOMHOG000223248.
KOK00765.
OMADVRLIIV.
OrthoDBEOG66MQT3.

Enzyme and pathway databases

BioCycCPHY357809:GHCL-2828-MONOMER.
UniPathwayUPA00031; UER00006.

Family and domain databases

HAMAPMF_01018. HisG_Short.
InterProIPR013820. ATP_PRibTrfase_cat.
IPR018198. ATP_PRibTrfase_CS.
IPR001348. ATP_PRibTrfase_HisG.
IPR024893. ATP_PRibTrfase_HisG_short.
[Graphical view]
PANTHERPTHR21403. PTHR21403. 1 hit.
PfamPF01634. HisG. 1 hit.
[Graphical view]
TIGRFAMsTIGR00070. hisG. 1 hit.
PROSITEPS01316. ATP_P_PHORIBOSYLTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS1_CLOPH
AccessionPrimary (citable) accession number: A9KNX6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 47 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