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Protein

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

Gene

hisA

Organism
Bacillus clausii (strain KSM-K16)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Pathway:iL-histidine biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase 1 (hisD1), Histidinol dehydrogenase 2 (hisD2)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Proton acceptorUniRule annotation
Active sitei131 – 1311Proton donorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciBCLA66692:GHMP-3127-MONOMER.
UniPathwayiUPA00031; UER00009.

Names & Taxonomyi

Protein namesi
Recommended name:
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseUniRule annotation (EC:5.3.1.16UniRule annotation)
Alternative name(s):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomeraseUniRule annotation
Gene namesi
Name:hisAUniRule annotation
Ordered Locus Names:ABC3045
OrganismiBacillus clausii (strain KSM-K16)
Taxonomic identifieri66692 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001168 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2402401-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000141977Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi66692.ABC3045.

Structurei

3D structure databases

ProteinModelPortaliQ5WDI1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiEWLHLVD.
OrthoDBiEOG6H1Q3W.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00007. TIGR00007. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5WDI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYTIYPAID IRAGKCVRLE QGDYNKETIY GESPYKMAKS FQDAGAKWVH
60 70 80 90 100
VVDLDGAKAK RPVNDEAILT IAQKLDVPVQ VGGGIRTEQD IDRYINGGVA
110 120 130 140 150
RVVLGSVAVY QPDFTKQMLA KYGEQMAIGI DARDGYVATE GWLETSHVKA
160 170 180 190 200
EDLAAEMARF GAKTFIFTDI ARDGMLTGPN IEACVALSKA ANANVIASGG
210 220 230 240
VSSIADLAQL RAASLAGAIV GKALYTKRFT LEEALAEGEL
Length:240
Mass (Da):25,698
Last modified:November 23, 2004 - v1
Checksum:iAFCCDD88C1AC78B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD65579.1.
RefSeqiWP_011247887.1. NC_006582.1.

Genome annotation databases

EnsemblBacteriaiBAD65579; BAD65579; ABC3045.
KEGGibcl:ABC3045.
PATRICi18925804. VBIBacCla58185_3251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006627 Genomic DNA. Translation: BAD65579.1.
RefSeqiWP_011247887.1. NC_006582.1.

3D structure databases

ProteinModelPortaliQ5WDI1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi66692.ABC3045.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD65579; BAD65579; ABC3045.
KEGGibcl:ABC3045.
PATRICi18925804. VBIBacCla58185_3251.

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiEWLHLVD.
OrthoDBiEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciBCLA66692:GHMP-3127-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00007. TIGR00007. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
    Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KSM-K16.

Entry informationi

Entry nameiHIS4_BACSK
AccessioniPrimary (citable) accession number: Q5WDI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 23, 2004
Last modified: July 22, 2015
This is version 70 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.