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A0PP18 (HIS4_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:
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:MUL_1576
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in both the histidine and tryptophan biosynthetic pathways By similarity. 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. HAMAP-Rule MF_01014

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

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244Phosphoribosyl isomerase A HAMAP-Rule MF_01014
PRO_0000290569

Sites

Active site101Proton acceptor By similarity
Active site1291Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PP18 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 23FF4C7D18B9D9B2

FASTA24425,432
        10         20         30         40         50         60 
MPLILLPAVD VVEGRAVRLV QGKAGSETEY GSALDAALGW QRDGAEWIHL VDLDAAFGRG 

        70         80         90        100        110        120 
SNRELLAEVV GKLDVAVELS GGIRDDDSLA AALATGCARV NLGTAALENP QWCARMIAEH 

       130        140        150        160        170        180 
GEKVAVGLDV QIVGGKHRLR GRGWETDGGD LWEVLQRLDS EGCSRYVVTD VTKDGTLAGP 

       190        200        210        220        230        240 
NLELLAGVAG RTEAPVIASG GVSSLDDLRA IATLTGQGVE GAIVGKALYA GRFTLPQALT 


AVRE 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL04087.1.
RefSeqYP_905558.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PP18.
SMRA0PP18. Positions 3-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_1576.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL04087; ABL04087; MUL_1576.
GeneID4552312.
KEGGmul:MUL_1576.
PATRIC18170065. VBIMycUlc37413_1887.

Organism-specific databases

GenoListMUL_1576.
CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
K01817.
OMAQRDYGSD.
OrthoDBEOG6H1Q3W.

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...

Entry information

Entry nameHIS4_MYCUA
AccessionPrimary (citable) accession number: A0PP18
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: January 9, 2007
Last modified: May 14, 2014
This is version 49 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