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P50936 (HIS4_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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:RHOS4_08300
ORF Names:RSP_2243
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

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
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_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_0000142047

Sites

Active site81Proton acceptor By similarity
Active site1291Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
P50936 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 53081E982DE01BEC

FASTA23924,518
        10         20         30         40         50         60 
MILYPAIDLK DGQCVRLLRG EMEAATVFGD DPAAQAAAFE AAGCEWVHLV DLNGAFAGRP 

        70         80         90        100        110        120 
VNAAAVEAIL ARIAVPAQLG GGIRDMATIA LWLEKGLARV ILGTVAVENP GLVREAARAF 

       130        140        150        160        170        180 
PGRVAVGIDA RKGRVATKGW ATETDVMATD LARSFEDAGV AAIIYTDIDR DGAMAGPNIE 

       190        200        210        220        230 
ATDALARAVS IPVIASGGVS SLADLLALRD TGSIAGAISG RALYDGALDL TQALQALRA 

« Hide

References

« Hide 'large scale' references
[1]Oriol E.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87256 Genomic DNA. Translation: CAA60709.1.
CP000143 Genomic DNA. Translation: ABA78398.1.
PIRS54837.
RefSeqYP_352299.1. NC_007493.2.

3D structure databases

ProteinModelPortalP50936.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_2243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA78398; ABA78398; RSP_2243.
GeneID3719773.
KEGGrsp:RSP_2243.
PATRIC23151504. VBIRhoSph57909_1146.

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAGWAEETD.
OrthoDBEOG6H1Q3W.
PhylomeDBP50936.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-854-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_RHOS4
AccessionPrimary (citable) accession number: P50936
Secondary accession number(s): Q3J486
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 93 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