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Q5X5X3 (HIS4_LEGPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

EC=5.3.1.16
Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene names
Name:hisA
Ordered Locus Names:lpp1197
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_01014

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   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_function1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2392391-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142014

Sites

Active site81Proton acceptor By similarity
Active site1291Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X5X3 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 9C9E7CDC664AA133

FASTA23926,356
        10         20         30         40         50         60 
MLVIPAIDLQ SGRCVRLKQG RFDQVTQFSV FPIERALHFA KLGAKRLHVV DLDGARSGKM 

        70         80         90        100        110        120 
QQLELICSMQ KTGIPIQAGG GIRSIEQALE CSNAGISQLV IGSLAITNPD LTIQIIEKIK 

       130        140        150        160        170        180 
PENIVLALDV RVDTKVPLLA INGWQNNSTS SLWEVVSYYE NYGIKNILCT DIACDGMMNG 

       190        200        210        220        230 
PNFDLYQQAV EYFPQIAWQA SGGVRHMQDI TTLNSLGISA VILGLMLYQD NVNFEELLC 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Paris.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR628336 Genomic DNA. Translation: CAH12348.1.
RefSeqYP_123521.1. NC_006368.1.

3D structure databases

ProteinModelPortalQ5X5X3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING297246.lpp1197.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH12348; CAH12348; lpp1197.
GeneID3118673.
KEGGlpp:lpp1197.
PATRIC22322739. VBILegPne27771_1430.

Organism-specific databases

LegioListlpp1197.
CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAKIAVSGW.
OrthoDBEOG6H1Q3W.
ProtClustDBCLSK832673.

Enzyme and pathway databases

BioCycLPNE297246:GCO9-1533-MONOMER.
UniPathwayUPA00031; UER00009.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00007. TIGR00007. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_LEGPA
AccessionPrimary (citable) accession number: Q5X5X3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 23, 2004
Last modified: February 19, 2014
This is version 64 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