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P40545 (HIS4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

EC=5.3.1.16
Alternative name(s):
5-proFAR isomerase
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene names
Name:HIS6
Ordered Locus Names:YIL020C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR.

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.

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Present with 6490 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the HisA/HisF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2612611-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
PRO_0000141963

Experimental info

Sequence conflict2431F → S in AAS56185. Ref.4

Secondary structure

............................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40545 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: FA33F3A8ED52B526

FASTA26129,557
        10         20         30         40         50         60 
MTKFIGCIDL HNGEVKQIVG GTLTSKKEDV PKTNFVSQHP SSYYAKLYKD RDVQGCHVIK 

        70         80         90        100        110        120 
LGPNNDDAAR EALQESPQFL QVGGGINDTN CLEWLKWASK VIVTSWLFTK EGHFQLKRLE 

       130        140        150        160        170        180 
RLTELCGKDR IVVDLSCRKT QDGRWIVAMN KWQTLTDLEL NADTFRELRK YTNEFLIHAA 

       190        200        210        220        230        240 
DVEGLCGGID ELLVSKLFEW TKDYDDLKIV YAGGAKSVDD LKLVDELSHG KVDLTFGSSL 

       250        260 
DIFGGNLVKF EDCCRWNEKQ G 

« Hide

References

« Hide 'large scale' references
[1]"Paralogous histidine biosynthetic genes: evolutionary analysis of the Saccharomyces cerevisiae HIS6 and HIS7 genes."
Fani R., Tamburini E., Mori E., Lazcano A., Lio P., Barberio C., Casalone E., Cavalieri D., Perito B., Polsinelli M.
Gene 197:9-17(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: YNN 282.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. expand/collapse author list , Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Crystal structure of the yeast His6 enzyme suggests a reaction mechanism."
Quevillon-Cheruel S., Leulliot N., Graille M., Blondeau K., Janin J., van Tilbeurgh H.
Protein Sci. 15:1516-1521(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 2-261.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87341 Genomic DNA. Translation: CAA60779.1.
Z46881 Genomic DNA. Translation: CAA86972.1.
AY557859 Genomic DNA. Translation: AAS56185.1.
BK006942 Genomic DNA. Translation: DAA08525.1.
PIRS49962.
RefSeqNP_012244.3. NM_001179370.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGKX-ray1.30A2-261[»]
ProteinModelPortalP40545.
SMRP40545. Positions 2-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34968. 16 interactions.
DIPDIP-4716N.
IntActP40545. 1 interaction.
MINTMINT-561085.
STRING4932.YIL020C.

Proteomic databases

MaxQBP40545.
PaxDbP40545.
PeptideAtlasP40545.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYIL020C; YIL020C; YIL020C.
GeneID854792.
KEGGsce:YIL020C.

Organism-specific databases

CYGDYIL020c.
SGDS000001282. HIS6.

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000172261.
KOK01814.
OMAFVAMNKW.
OrthoDBEOG7ZWDC9.

Enzyme and pathway databases

BioCycYEAST:YIL020C-MONOMER.
BRENDA5.3.1.16. 984.
UniPathwayUPA00031; UER00009.

Gene expression databases

GenevestigatorP40545.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR011858. HisA_euk.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERPTHR21169. PTHR21169. 1 hit.
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR02129. hisA_euk. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP40545.
NextBio977588.

Entry information

Entry nameHIS4_YEAST
AccessionPrimary (citable) accession number: P40545
Secondary accession number(s): D6VVQ9, Q6Q5P5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways