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

A1WR23 (HIS4_VEREI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Veis_4377
OrganismVerminephrobacter eiseniae (strain EF01-2) [Complete proteome] [HAMAP]
Taxonomic identifier391735 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeVerminephrobacter

Protein attributes

Sequence length245 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 – 2452451-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000290560

Sites

Active site81Proton acceptor By similarity
Active site1311Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WR23 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 939BBD68986E0728

FASTA24525,754
        10         20         30         40         50         60 
MLLIPAIDLK DGHCVRLRQG DMDQSTTFGE NPAAMARQWI DAGARRLHLV DLNGALAGMP 

        70         80         90        100        110        120 
KNYGAIKSIL KEVGDDIPVQ LGGGIRDLDT IEKYIDGGLR YVIIGTAAVK NPGFLKDACS 

       130        140        150        160        170        180 
AFGGHIIVGL DARDGKVATD GWSKLTGHGV VDLARKFEDW GVESIIYTDI GRDGMLSGIN 

       190        200        210        220        230        240 
IDATVALAQA LSIPVIASGG LSGMADIEQL CAVQDEGIEG VICGRAIYSG DLDFAAAQAR 


ADEMG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EF01-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000542 Genomic DNA. Translation: ABM60080.1.
RefSeqYP_999098.1. NC_008786.1.

3D structure databases

ProteinModelPortalA1WR23.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391735.Veis_4377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM60080; ABM60080; Veis_4377.
GeneID4693230.
KEGGvei:Veis_4377.
PATRIC24022659. VBIVerEis120356_4701.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMACARYVVT.
OrthoDBEOG6H1Q3W.

Enzyme and pathway databases

BioCycVEIS391735:GHY5-4429-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_VEREI
AccessionPrimary (citable) accession number: A1WR23
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 45 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