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Protein

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase

Gene

HIS6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

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.

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 (HIS1)
  2. Histidine biosynthesis trifunctional protein (HIS4)
  3. Histidine biosynthesis trifunctional protein (HIS4)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (HIS6)
  5. Imidazole glycerol phosphate synthase hisHF (HIS7)
  6. Imidazoleglycerol-phosphate dehydratase (HIS3)
  7. Histidinol-phosphate aminotransferase (HIS5)
  8. Histidinol-phosphatase (HIS2)
  9. Histidine biosynthesis trifunctional protein (HIS4)
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.

GO - Molecular functioni

GO - Biological processi

  • histidine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciYEAST:YIL020C-MONOMER.
BRENDAi5.3.1.16. 984.
UniPathwayiUPA00031; UER00009.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:HIS6
Ordered Locus Names:YIL020C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL020C.
SGDiS000001282. HIS6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001419631 – 2611-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST261

Proteomic databases

MaxQBiP40545.
PRIDEiP40545.

Interactioni

Protein-protein interaction databases

BioGridi34968. 17 interactors.
DIPiDIP-4716N.
IntActiP40545. 1 interactor.
MINTiMINT-561085.

Structurei

Secondary structure

1261
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Helixi41 – 50Combined sources10
Beta strandi57 – 64Combined sources8
Helixi66 – 75Combined sources10
Turni77 – 79Combined sources3
Beta strandi80 – 85Combined sources6
Turni88 – 90Combined sources3
Helixi91 – 94Combined sources4
Turni95 – 97Combined sources3
Beta strandi101 – 103Combined sources3
Helixi105 – 107Combined sources3
Helixi116 – 126Combined sources11
Helixi128 – 130Combined sources3
Beta strandi131 – 141Combined sources11
Beta strandi144 – 149Combined sources6
Turni150 – 153Combined sources4
Beta strandi154 – 161Combined sources8
Helixi162 – 168Combined sources7
Turni169 – 171Combined sources3
Beta strandi173 – 178Combined sources6
Helixi191 – 201Combined sources11
Beta strandi208 – 213Combined sources6
Helixi220 – 228Combined sources9
Beta strandi232 – 235Combined sources4
Helixi241 – 243Combined sources3
Beta strandi246 – 248Combined sources3
Helixi250 – 260Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGKX-ray1.30A2-261[»]
ProteinModelPortaliP40545.
SMRiP40545.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40545.

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

HOGENOMiHOG000172261.
InParanoidiP40545.
KOiK01814.
OMAiNKWQTLT.
OrthoDBiEOG092C43NB.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR011858. HisA_euk.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR02129. hisA_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

P40545-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKFIGCIDL HNGEVKQIVG GTLTSKKEDV PKTNFVSQHP SSYYAKLYKD
60 70 80 90 100
RDVQGCHVIK LGPNNDDAAR EALQESPQFL QVGGGINDTN CLEWLKWASK
110 120 130 140 150
VIVTSWLFTK EGHFQLKRLE RLTELCGKDR IVVDLSCRKT QDGRWIVAMN
160 170 180 190 200
KWQTLTDLEL NADTFRELRK YTNEFLIHAA DVEGLCGGID ELLVSKLFEW
210 220 230 240 250
TKDYDDLKIV YAGGAKSVDD LKLVDELSHG KVDLTFGSSL DIFGGNLVKF
260
EDCCRWNEKQ G
Length:261
Mass (Da):29,557
Last modified:February 1, 1995 - v1
Checksum:iFA33F3A8ED52B526
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti243F → S in AAS56185 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87341 Genomic DNA. Translation: CAA60779.1.
Z46881 Genomic DNA. Translation: CAA86972.1.
AY557859 Genomic DNA. Translation: AAS56185.1.
BK006942 Genomic DNA. Translation: DAA08525.1.
PIRiS49962.
RefSeqiNP_012244.3. NM_001179370.3.

Genome annotation databases

EnsemblFungiiYIL020C; YIL020C; YIL020C.
GeneIDi854792.
KEGGisce:YIL020C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87341 Genomic DNA. Translation: CAA60779.1.
Z46881 Genomic DNA. Translation: CAA86972.1.
AY557859 Genomic DNA. Translation: AAS56185.1.
BK006942 Genomic DNA. Translation: DAA08525.1.
PIRiS49962.
RefSeqiNP_012244.3. NM_001179370.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AGKX-ray1.30A2-261[»]
ProteinModelPortaliP40545.
SMRiP40545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34968. 17 interactors.
DIPiDIP-4716N.
IntActiP40545. 1 interactor.
MINTiMINT-561085.

Proteomic databases

MaxQBiP40545.
PRIDEiP40545.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL020C; YIL020C; YIL020C.
GeneIDi854792.
KEGGisce:YIL020C.

Organism-specific databases

EuPathDBiFungiDB:YIL020C.
SGDiS000001282. HIS6.

Phylogenomic databases

HOGENOMiHOG000172261.
InParanoidiP40545.
KOiK01814.
OMAiNKWQTLT.
OrthoDBiEOG092C43NB.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciYEAST:YIL020C-MONOMER.
BRENDAi5.3.1.16. 984.

Miscellaneous databases

EvolutionaryTraceiP40545.
PROiP40545.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR011858. HisA_euk.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR02129. hisA_euk. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHIS4_YEAST
AccessioniPrimary (citable) accession number: P40545
Secondary accession number(s): D6VVQ9, Q6Q5P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6490 molecules/cell in log phase SD medium.1 Publication

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
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

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.