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P16250 (HIS4_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Phosphoribosyl isomerase A
Alternative name(s):
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
EC=5.3.1.16
N-(5'-phosphoribosyl)anthranilate isomerase
Short name=PRAI
EC=5.3.1.24
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene names
Name:priA
Synonyms:hisA
Ordered Locus Names:SCO2050
ORF Names:SC4G6.19c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for histidine and the isomerization of the aminoaldose PRA to the aminoketose CdRP in the biosynthsis pathway for tryptophan. HAMAP-Rule MF_01014

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. Ref.4

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. Ref.4

Pathway

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

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_01014

Subunit structure

Monomer. Ref.4

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Biophysicochemical properties

Kinetic parameters:

KM=28 µM for ProFAR Ref.4

KM=4 µM for PRA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Phosphoribosyl isomerase A HAMAP-Rule MF_01014
PRO_0000142087

Sites

Active site111Proton acceptor By similarity
Active site1301Proton donor By similarity

Experimental info

Mutagenesis111D → A: No activity. Ref.5
Mutagenesis191R → A: No effect on activity toward PRA. No activity toward ProFAR. Ref.5
Mutagenesis811S → T: No activity toward PRA. Almost no effect on activity toward ProFAR. Ref.5
Mutagenesis1301D → A: Very low activity toward PRA. No activity toward ProFAR. Ref.5
Mutagenesis1301D → Q: No activity. Ref.5
Mutagenesis1661T → A: No activity. Ref.5
Mutagenesis1711D → A: Low activity toward PRA. No activity toward ProFAR. Ref.5

Secondary structure

.............................................. 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16250 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: A150E831DDABC76F

FASTA24025,080
        10         20         30         40         50         60 
MSKLELLPAV DVRDGQAVRL VHGESGTETS YGSPLEAALA WQRSGAEWLH LVDLDAAFGT 

        70         80         90        100        110        120 
GDNRALIAEV AQAMDIKVEL SGGIRDDDTL AAALATGCTR VNLGTAALET PEWVAKVIAE 

       130        140        150        160        170        180 
HGDKIAVGLD VRGTTLRGRG WTRDGGDLYE TLDRLNKEGC ARYVVTDIAK DGTLQGPNLE 

       190        200        210        220        230        240 
LLKNVCAATD RPVVASGGVS SLDDLRAIAG LVPAGVEGAI VGKALYAKAF TLEEALEATS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)."
Limauro D., Avitabile A., Cappellano M., Puglia A.M., Bruni C.B.
Gene 90:31-41(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A3(2) / NRRL B-16638.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[3]"Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis."
Barona-Gomez F., Hodgson D.A.
EMBO Rep. 4:296-300(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HISTIDINE AND TRYPTOPHAN BIOSYNTHESIS.
Strain: ATCC BAA-471 / A3(2) / M145.
[4]"Two-fold repeated (beta alpha)4 half-barrels may provide a molecular tool for dual substrate specificity."
Kuper J., Doenges C., Wilmanns M.
EMBO Rep. 6:134-139(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[5]"The structure/function relationship of a dual-substrate (beta alpha)8-isomerase."
Wright H., Noda-Garcia L., Ochoa-Leyva A., Hodgson D.A., Fueloep V., Barona-Gomez F.
Biochem. Biophys. Res. Commun. 365:16-21(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS OF ASP-11; ARG-19; SER-81; ASP-130; THR-166 AND ASP-171.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31628 Genomic DNA. Translation: AAA26760.1.
AL939111 Genomic DNA. Translation: CAB51442.1.
PIRJQ0641.
RefSeqNP_626310.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZWX-ray1.80A1-240[»]
2VEPX-ray1.80A1-240[»]
2X30X-ray1.95A1-240[»]
ProteinModelPortalP16250.
SMRP16250. Positions 1-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO2050.

Proteomic databases

PRIDEP16250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB51442; CAB51442; CAB51442.
GeneID1097484.
KEGGsco:SCO2050.
PATRIC23733744. VBIStrCoe124346_2081.

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
K01817.
OMACARYVVT.
OrthoDBEOG6H1Q3W.
PhylomeDBP16250.
ProtClustDBPRK14024.

Enzyme and pathway databases

UniPathwayUPA00031; UER00009.
UPA00035; UER00042.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01919. hisA-trpF. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP16250.

Entry information

Entry nameHIS4_STRCO
AccessionPrimary (citable) accession number: P16250
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 113 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways