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P10372 (HIS4_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene names
Name:hisA
Ordered Locus Names:STM2076
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length245 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014

Subcellular location

Cytoplasm HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2452451-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142049

Sites

Active site71Proton acceptor By similarity
Active site1291Proton donor By similarity

Experimental info

Sequence conflict123 – 1242AL → GV in CAA31827. Ref.1
Sequence conflict1351H → Q in CAA31827. Ref.1
Sequence conflict1771G → A in CAA31827. Ref.1
Sequence conflict2111I → DV Ref.1
Sequence conflict2221V → M in CAA31827. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P10372 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 20CF123F43DCE925

FASTA24526,089
        10         20         30         40         50         60 
MIIPALDLID GTVVRLHQGD YARQRDYGND PLPRLQDYAA QGAGVLHLVD LTGAKDPAKR 

        70         80         90        100        110        120 
QIPLIKTLVA GVNVPVQVGG GVRTEEDVAA LLKAGVARVV IGSTAVKSPD VVKGWFERFG 

       130        140        150        160        170        180 
AQALVLALDV RIDEHGTKQV AVSGWQENSG VSLEQLVETY LPVGLKHVLC TDISRDGTLA 

       190        200        210        220        230        240 
GSNVSLYEEV CARYPQIAFQ SSGGIGDIDD IAALRGTGVR GVIVGRALLE GKFTVKEAIQ 


CWQNV 

« Hide

References

« Hide 'large scale' references
[1]"Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons."
Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.
J. Mol. Biol. 203:585-606(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13464 Genomic DNA. Translation: CAA31827.1.
AE006468 Genomic DNA. Translation: AAL20980.1.
PIRISEBIC. JS0161.
RefSeqNP_461021.1. NC_003197.1.

3D structure databases

ProteinModelPortalP10372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2076.

Proteomic databases

PRIDEP10372.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20980; AAL20980; STM2076.
GeneID1253597.
KEGGstm:STM2076.
PATRIC32382735. VBISalEnt20916_2198.

Phylogenomic databases

HOGENOMHOG000224614.
KOK01814.
OMACARYVVT.
OrthoDBEOG6H1Q3W.
ProtClustDBPRK00748.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2088-MONOMER.
UniPathwayUPA00031; UER00009.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00007. TIGR00007. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_SALTY
AccessionPrimary (citable) accession number: P10372
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2002
Last modified: February 19, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways