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A5U2V9 (HIS4_MYCTA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:MRA_1613
OrganismMycobacterium tuberculosis (strain ATCC 25177 / H37Ra) [Complete proteome] [HAMAP]
Taxonomic identifier419947 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length245 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 – 245245Phosphoribosyl isomerase A HAMAP-Rule MF_01014
PRO_1000063221

Sites

Active site111Proton acceptor By similarity
Active site1301Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A5U2V9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 906C2C40268C3257

FASTA24525,763
        10         20         30         40         50         60 
MMPLILLPAV DVVEGRAVRL VQGKAGSQTE YGSAVDAALG WQRDGAEWIH LVDLDAAFGR 

        70         80         90        100        110        120 
GSNHELLAEV VGKLDVQVEL SGGIRDDESL AAALATGCAR VNVGTAALEN PQWCARVIGE 

       130        140        150        160        170        180 
HGDQVAVGLD VQIIDGEHRL RGRGWETDGG DLWDVLERLD SEGCSRFVVT DITKDGTLGG 

       190        200        210        220        230        240 
PNLDLLAGVA DRTDAPVIAS GGVSSLDDLR AIATLTHRGV EGAIVGKALY ARRFTLPQAL 


AAVRD 

« Hide

References

[1]"Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25177 / H37Ra.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000611 Genomic DNA. Translation: ABQ73359.1.
RefSeqYP_001282921.1. NC_009525.1.

3D structure databases

ProteinModelPortalA5U2V9.
SMRA5U2V9. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING419947.MRA_1613.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ73359; ABQ73359; MRA_1613.
GeneID5211626.
KEGGmra:MRA_1613.
PATRIC18143179. VBIMycTub106795_1792.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMTUB419947:GJ8N-1663-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_MYCTA
AccessionPrimary (citable) accession number: A5U2V9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 47 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