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A4SV19 (HIS4_POLSQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:Pnuc_0111
OrganismPolynucleobacter necessarius subsp. asymbioticus (strain DSM 18221 / CIP 109841 / QLW-P1DMWA-1) [Complete proteome] [HAMAP]
Taxonomic identifier312153 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaePolynucleobacter

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
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_1000084103

Sites

Active site81Proton acceptor By similarity
Active site1311Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SV19 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: FD7C5EB958120C54

FASTA25326,950
        10         20         30         40         50         60 
MLLIPAIDLK DGHCVRLEQG DMDKATVFSE DPGAMAAHWI SKGARRLHLV DLNGAFAGKL 

        70         80         90        100        110        120 
KNESAIKSIL KAVGNEIPVQ LGGGIRDLET IERLLDDGIS TVIIGTAAVK NPGFVQDACT 

       130        140        150        160        170        180 
AFPGHVMVGL DARDGKVATD GWSKITGHEV IDLAKKFEDW GVEAIIYTDI GRDGMLKGVN 

       190        200        210        220        230        240 
IEATMKLAQA IRIPVIASGG LSNNQDIEAL CKAEEEGVMG VIAGRSIYAA DLDLAAAQKY 

       250 
ADELTLKYAK KII 

« Hide

References

[1]"Complete genome sequence of Polynucleobacter necessarius subsp. asymbioticus type strain (QLW-P1DMWA-1(T))."
Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.
Stand. Genomic Sci. 6:74-83(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 18221 / CIP 109841 / QLW-P1DMWA-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000655 Genomic DNA. Translation: ABP33333.1.
RefSeqYP_001154897.1. NC_009379.1.

3D structure databases

ProteinModelPortalA4SV19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING312153.Pnuc_0111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP33333; ABP33333; Pnuc_0111.
GeneID5053361.
KEGGpnu:Pnuc_0111.
PATRIC22964565. VBIPolNec12025_0116.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAQRDYGSD.
OrthoDBEOG6H1Q3W.

Enzyme and pathway databases

BioCycPNEC312153:GH50-121-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_POLSQ
AccessionPrimary (citable) accession number: A4SV19
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: May 14, 2014
This is version 48 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