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Protein

Phosphoribosyl isomerase A

Gene

priA

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in both the histidine and tryptophan biosynthetic pathways.

Catalytic activityi

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

Pathwayi: L-histidine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE), Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI), Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. Phosphoribosyl isomerase A (priA), Phosphoribosyl isomerase A (priA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Histidinol-phosphatase (hisN)
  9. Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. Phosphoribosyl isomerase A (priA), Phosphoribosyl isomerase A (priA)
  4. Indole-3-glycerol phosphate synthase (trpC), Indole-3-glycerol phosphate synthase (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Proton acceptorBy similarity
Active sitei129 – 1291Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

  • growth Source: MTBBASE
  • histidine biosynthetic process Source: MTBBASE
  • tryptophan biosynthetic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Histidine biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
UPA00035; UER00042.

Names & Taxonomyi

Protein namesi
Recommended 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 (EC:5.3.1.24)
Short name:
PRAI
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene namesi
Name:priA
Synonyms:hisA
Ordered Locus Names:Rv1603
ORF Names:MTCY336.01c, MTV046.01
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv1603.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 244244Phosphoribosyl isomerase APRO_0000142085Add
BLAST

Proteomic databases

PaxDbiP9WMM5.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv1603.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Beta strandi15 – 184Combined sources
Helixi24 – 263Combined sources
Beta strandi28 – 325Combined sources
Helixi33 – 4210Combined sources
Beta strandi46 – 527Combined sources
Helixi53 – 564Combined sources
Helixi63 – 7210Combined sources
Beta strandi74 – 829Combined sources
Helixi86 – 938Combined sources
Turni94 – 963Combined sources
Beta strandi98 – 1025Combined sources
Helixi104 – 1085Combined sources
Helixi110 – 12011Combined sources
Helixi121 – 1233Combined sources
Beta strandi124 – 13310Combined sources
Beta strandi136 – 1416Combined sources
Turni142 – 1454Combined sources
Beta strandi146 – 1505Combined sources
Helixi151 – 16010Combined sources
Beta strandi166 – 1705Combined sources
Turni171 – 1777Combined sources
Helixi182 – 1898Combined sources
Beta strandi196 – 2005Combined sources
Helixi205 – 2128Combined sources
Helixi213 – 2175Combined sources
Beta strandi219 – 2246Combined sources
Helixi226 – 2294Combined sources
Helixi235 – 2417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y85X-ray2.40A/B/C/D1-244[»]
2Y88X-ray1.33A1-244[»]
2Y89X-ray2.50A1-244[»]
3ZS4X-ray1.90A1-244[»]
ProteinModelPortaliP9WMM5.
SMRiP9WMM5. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
KOiK01814.
K01817.
OMAiEWLHLVD.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WMM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLILLPAVD VVEGRAVRLV QGKAGSQTEY GSAVDAALGW QRDGAEWIHL
60 70 80 90 100
VDLDAAFGRG SNHELLAEVV GKLDVQVELS GGIRDDESLA AALATGCARV
110 120 130 140 150
NVGTAALENP QWCARVIGEH GDQVAVGLDV QIIDGEHRLR GRGWETDGGD
160 170 180 190 200
LWDVLERLDS EGCSRFVVTD ITKDGTLGGP NLDLLAGVAD RTDAPVIASG
210 220 230 240
GVSSLDDLRA IATLTHRGVE GAIVGKALYA RRFTLPQALA AVRD
Length:244
Mass (Da):25,632
Last modified:April 16, 2014 - v1
Checksum:i8B9C2C403958A01E
GO

Sequence cautioni

The sequence CCP44367 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44367.1. Different initiation.
PIRiE70544.
RefSeqiNP_216119.1. NC_000962.3.
WP_003407955.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP44367; CCP44367; Rv1603.
GeneIDi885873.
KEGGimtu:Rv1603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP44367.1. Different initiation.
PIRiE70544.
RefSeqiNP_216119.1. NC_000962.3.
WP_003407955.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y85X-ray2.40A/B/C/D1-244[»]
2Y88X-ray1.33A1-244[»]
2Y89X-ray2.50A1-244[»]
3ZS4X-ray1.90A1-244[»]
ProteinModelPortaliP9WMM5.
SMRiP9WMM5. Positions 1-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv1603.

Proteomic databases

PaxDbiP9WMM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP44367; CCP44367; Rv1603.
GeneIDi885873.
KEGGimtu:Rv1603.

Organism-specific databases

TubercuListiRv1603.

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
KOiK01814.
K01817.
OMAiEWLHLVD.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
UPA00035; UER00042.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHIS4_MYCTU
AccessioniPrimary (citable) accession number: P9WMM5
Secondary accession number(s): L0T7E1, O06588, P60578
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: September 7, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.