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A3Q127 (HIS4_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Mjls_3075
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length248 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 – 248248Phosphoribosyl isomerase A HAMAP-Rule MF_01014
PRO_0000290566

Sites

Active site141Proton acceptor By similarity
Active site1331Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A3Q127 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 1A2CBB2F54221470

FASTA24826,204
        10         20         30         40         50         60 
MSEKRPLILL PAVDVVEGRA VRLVQGKAGS ETEYGSALDA ALGWQRDGAE WIHLVDLDAA 

        70         80         90        100        110        120 
FGRGSNRELL ADVVGRLDVA VELSGGIRDD ESLEAALATG CARVNIGTAA LENPQWCAKV 

       130        140        150        160        170        180 
VAEFGDKVAV GLDVKIVDDQ HRLRGRGWET DGGDLWEVLD RLDSEGCSRY VVTDVTKDGT 

       190        200        210        220        230        240 
LQGPNLDLLG RVADRTDAPV IASGGVSSLD DLRAIATLTD RGVEGAIVGK ALYAGRFTLP 


EALAAMGQ 

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000580 Genomic DNA. Translation: ABN98854.1.
RefSeqYP_001071345.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3Q127.
SMRA3Q127. Positions 7-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164757.Mjls_3075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN98854; ABN98854; Mjls_3075.
GeneID4878788.
KEGGmjl:Mjls_3075.
PATRIC18092333. VBIMycSp51234_3096.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMSP164757:GHV3-3094-MONOMER.
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_MYCSJ
AccessionPrimary (citable) accession number: A3Q127
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: April 3, 2007
Last modified: February 19, 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