Phosphoribosyl isomerase A - Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

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P16250 (HIS4_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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
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

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces ›

Protein attributes

Sequence length	240 AA.
Sequence status	Complete.
Protein existence	Evidence 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-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)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.
Sequence similarities	Belongs to the HisA/HisF family.
Biophysicochemical properties	Kinetic parameters: K_M=28 µM for ProFAR Ref.4 K_M=4 µM for PRA

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Histidine biosynthesis Tryptophan biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP tryptophan biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylanthranilate isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 240

240

Phosphoribosyl isomerase A HAMAP-Rule MF_01014

PRO_0000142087

Sites

Active site

Proton acceptor By similarity

Active site

130

Proton donor By similarity

Experimental info

Mutagenesis

D → A: No activity. Ref.5

Mutagenesis

R → A: No effect on activity toward PRA. No activity toward ProFAR. Ref.5

Mutagenesis

S → T: No activity toward PRA. Almost no effect on activity toward ProFAR. Ref.5

Mutagenesis

130

D → A: Very low activity toward PRA. No activity toward ProFAR. Ref.5

Mutagenesis

130

D → Q: No activity. Ref.5

Mutagenesis

166

T → A: No activity. Ref.5

Mutagenesis

171

D → A: Low activity toward PRA. No activity toward ProFAR. Ref.5

Secondary structure

240

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P16250 [UniParc].

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

FASTA

240

25,080

        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' referencesShow '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. 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.

PIR

JQ0641.

RefSeq

NP_626310.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VZW	X-ray	1.80	A	1-240	[»]
2VEP	X-ray	1.80	A	1-240	[»]
2X30	X-ray	1.95	A	1-240	[»]

ProteinModelPortal

P16250.

SMR

P16250. Positions 1-240.

ModBase

Search...

Protein-protein interaction databases

STRING

100226.SCO2050.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB51442; CAB51442; CAB51442.

GeneID

1097484.

KEGG

sco:SCO2050.

PATRIC

23733744. VBIStrCoe124346_2081.

Phylogenomic databases

eggNOG

COG0106.

HOGENOM

HOG000224614.

K01814.
K01817.

OMA

CARYVVT.

ProtClustDB

PRK14024.

Enzyme and pathway databases

UniPathway

UPA00031; UER00009.
UPA00035; UER00042.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_01014. HisA.

InterPro

IPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]

Pfam

PF00977. His_biosynth. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 1 hit.

TIGRFAMs

TIGR01919. hisA-trpF. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P16250.

Entry information

Entry name

HIS4_STRCO

Accession

Primary (citable) accession number: P16250

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents