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Q82AA1 (HIS4_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 78. 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:SAV_6158
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces ›

Protein attributes

Sequence length242 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 – 242242Phosphoribosyl isomerase A HAMAP-Rule MF_01014
PRO_0000142086

Sites

Active site121Proton acceptor By similarity
Active site1311Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82AA1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 9832F3C7F82E12F7

FASTA24225,264
        10         20         30         40         50         60 
MASKLELLPA VDVRDGQAVR LVHGESGTET SYGSPLEAAL AWQRSGAEWL HLVDLDAAFG 

        70         80         90        100        110        120 
TGDNRALIAE VAGAMDIKVE LSGGIRDDDT LAAALATGCT RVNLGTAALE TPEWVAKVIA 

       130        140        150        160        170        180 
EHGDKIAVGL DVRGTTLRGR GWTRDGGDLY ETLERLNSEG CARYVVTDIA KDGTLQGPNL 

       190        200        210        220        230        240 
ELLRNVCAAT DRPVVASGGV SSLDDLRAIA ALVPLGVEGS IVGKALYAKA FTLEEALEAV 


AK

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References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000030 Genomic DNA. Translation: BAC73869.1.
RefSeqNP_827334.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82AA1.
SMRQ82AA1. Positions 3-241.
ModBaseSearch...

Protein-protein interaction databases

STRING227882.SAV_6158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC73869; BAC73869; SAV_6158.
GeneID1211420.
KEGGsma:SAV_6158.
PATRIC23726354. VBIStrAve112782_6530.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSAVE227882:GJU1-6238-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. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR01919. hisA-trpF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_STRAW
AccessionPrimary (citable) accession number: Q82AA1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: May 29, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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