Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7UG70 (HIS4_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 72. 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:RB8080
OrganismRhodopirellula baltica (strain SH1) [Reference proteome] [HAMAP]
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length253 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 – 2532531-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142045

Sites

Active site191Proton acceptor By similarity
Active site1411Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UG70 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 5B09803229D1803B

FASTA25327,502
        10         20         30         40         50         60 
MSSQTPGSEP RMEIWPAIDL RHGKPVRLRQ GDYDQQTTFG DDPVEFAKRW QESGAKRLHL 

        70         80         90        100        110        120 
VDLDAARGDS PDANRDAVQR IIEATGLPCQ MGGGVRDEIT IESLLNVGVT RLVVGSRALK 

       130        140        150        160        170        180 
DPDWFVEMCD KYPGKLVAGI DARDGKVATQ GWLETSDVSA FEFATKLRSR TENIAAIVYT 

       190        200        210        220        230        240 
DIAKDGMMQG PNFEGLAEMA AASDIPLVAS GGVTTYDDIK QLVEMKMPAA IVGRSLYDGV 

       250 
MELGEVVRLA GDV 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294147 Genomic DNA. Translation: CAD78459.1.
RefSeqNP_868181.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UG70.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243090.RB8080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD78459; CAD78459; RB8080.
GeneID1792914.
KEGGrba:RB8080.
PATRIC23249271. VBIRhoBal59814_3904.

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAKIAVSGW.
OrthoDBEOG6H1Q3W.
ProtClustDBCLSK2759335.

Enzyme and pathway databases

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_RHOBA
AccessionPrimary (citable) accession number: Q7UG70
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 72 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