Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16250

- HIS4_STRCO

UniProt

P16250 - HIS4_STRCO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Phosphoribosyl isomerase A

Gene

priA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

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

Kineticsi

  1. KM=28 µM for ProFAR1 Publication
  2. KM=4 µM for PRA1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Proton acceptorBy similarity
Active sitei130 – 1301Proton donorBy similarity

GO - Molecular functioni

  1. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Source: UniProtKB-HAMAP
  2. phosphoribosylanthranilate isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
  2. tryptophan biosynthetic process Source: UniProtKB-HAMAP
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:SCO2050
ORF Names:SC4G6.19c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
ProteomesiUP000001973: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111D → A: No activity. 1 Publication
Mutagenesisi19 – 191R → A: No effect on activity toward PRA. No activity toward ProFAR. 1 Publication
Mutagenesisi81 – 811S → T: No activity toward PRA. Almost no effect on activity toward ProFAR. 1 Publication
Mutagenesisi130 – 1301D → A: Very low activity toward PRA. No activity toward ProFAR. 1 Publication
Mutagenesisi130 – 1301D → Q: No activity. 1 Publication
Mutagenesisi166 – 1661T → A: No activity. 1 Publication
Mutagenesisi171 – 1711D → A: Low activity toward PRA. No activity toward ProFAR. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Phosphoribosyl isomerase APRO_0000142087Add
BLAST

Proteomic databases

PRIDEiP16250.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi100226.SCO2050.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi16 – 183Combined sources
Beta strandi28 – 303Combined sources
Helixi34 – 4310Combined sources
Beta strandi47 – 537Combined sources
Helixi54 – 585Combined sources
Helixi64 – 7310Combined sources
Beta strandi75 – 839Combined sources
Helixi87 – 959Combined sources
Beta strandi99 – 1035Combined sources
Helixi105 – 1095Combined sources
Helixi111 – 12111Combined sources
Helixi122 – 1243Combined sources
Beta strandi125 – 1328Combined sources
Beta strandi139 – 1413Combined sources
Helixi148 – 15710Combined sources
Beta strandi163 – 1675Combined sources
Helixi168 – 1703Combined sources
Turni171 – 1733Combined sources
Helixi179 – 1879Combined sources
Beta strandi193 – 1975Combined sources
Helixi202 – 2098Combined sources
Turni210 – 2156Combined sources
Beta strandi216 – 2216Combined sources
Helixi223 – 2264Combined sources
Helixi232 – 2398Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZWX-ray1.80A1-240[»]
2VEPX-ray1.80A1-240[»]
2X30X-ray1.95A1-240[»]
ProteinModelPortaliP16250.
SMRiP16250. Positions 1-240.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16250.

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
InParanoidiP16250.
KOiK01814.
K01817.
OMAiQRDYGSD.
OrthoDBiEOG6H1Q3W.
PhylomeDBiP16250.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
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.

P16250-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKLELLPAV DVRDGQAVRL VHGESGTETS YGSPLEAALA WQRSGAEWLH
60 70 80 90 100
LVDLDAAFGT GDNRALIAEV AQAMDIKVEL SGGIRDDDTL AAALATGCTR
110 120 130 140 150
VNLGTAALET PEWVAKVIAE HGDKIAVGLD VRGTTLRGRG WTRDGGDLYE
160 170 180 190 200
TLDRLNKEGC ARYVVTDIAK DGTLQGPNLE LLKNVCAATD RPVVASGGVS
210 220 230 240
SLDDLRAIAG LVPAGVEGAI VGKALYAKAF TLEEALEATS
Length:240
Mass (Da):25,080
Last modified:August 1, 1990 - v1
Checksum:iA150E831DDABC76F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31628 Genomic DNA. Translation: AAA26760.1.
AL939111 Genomic DNA. Translation: CAB51442.1.
PIRiJQ0641.
RefSeqiNP_626310.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB51442; CAB51442; CAB51442.
GeneIDi1097484.
KEGGisco:SCO2050.
PATRICi23733744. VBIStrCoe124346_2081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31628 Genomic DNA. Translation: AAA26760.1 .
AL939111 Genomic DNA. Translation: CAB51442.1 .
PIRi JQ0641.
RefSeqi NP_626310.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P16250.
SMRi P16250. Positions 1-240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 100226.SCO2050.

Proteomic databases

PRIDEi P16250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB51442 ; CAB51442 ; CAB51442 .
GeneIDi 1097484.
KEGGi sco:SCO2050.
PATRICi 23733744. VBIStrCoe124346_2081.

Phylogenomic databases

eggNOGi COG0106.
HOGENOMi HOG000224614.
InParanoidi P16250.
KOi K01814.
K01817.
OMAi QRDYGSD.
OrthoDBi EOG6H1Q3W.
PhylomeDBi P16250.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00009 .
UPA00035 ; UER00042 .

Miscellaneous databases

EvolutionaryTracei P16250.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01014. HisA.
InterProi IPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view ]
Pfami PF00977. His_biosynth. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 1 hit.
TIGRFAMsi TIGR01919. hisA-trpF. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiHIS4_STRCO
AccessioniPrimary (citable) accession number: P16250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 26, 2014
This is version 117 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3