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Protein

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

Gene

hisA

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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.

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 (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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  9. Histidinol dehydrogenase (hisD)
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 sitei7 – 71Proton acceptorBy similarity
Active sitei129 – 1291Proton donorBy similarity

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

BioCyciSENT99287:GCTI-2088-MONOMER.
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):
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase
Gene namesi
Name:hisA
Ordered Locus Names:STM2076
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2452451-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000142049Add
BLAST

Proteomic databases

PaxDbiP10372.
PRIDEiP10372.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM2076.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Beta strandi12 – 165Combined sources
Helixi17 – 193Combined sources
Beta strandi23 – 264Combined sources
Helixi31 – 4010Combined sources
Beta strandi46 – 505Combined sources
Helixi51 – 555Combined sources
Helixi57 – 593Combined sources
Helixi62 – 709Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 816Combined sources
Helixi85 – 939Combined sources
Beta strandi97 – 1015Combined sources
Helixi103 – 1075Combined sources
Helixi109 – 11911Combined sources
Helixi121 – 1233Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi138 – 1425Combined sources
Turni143 – 1464Combined sources
Beta strandi147 – 1526Combined sources
Helixi153 – 1608Combined sources
Helixi161 – 1633Combined sources
Beta strandi167 – 1726Combined sources
Turni173 – 1775Combined sources
Helixi184 – 19310Combined sources
Beta strandi197 – 2037Combined sources
Helixi208 – 2125Combined sources
Turni213 – 2175Combined sources
Beta strandi220 – 2245Combined sources
Helixi226 – 2294Combined sources
Helixi235 – 24410Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A5WX-ray1.60A1-245[»]
5AHEX-ray1.70A1-245[»]
5AHFX-ray2.20A1-245[»]
5AHIX-ray2.00A1-245[»]
ProteinModelPortaliP10372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
HOGENOMiHOG000224614.
KOiK01814.
OMAiEWLHLVD.
OrthoDBiEOG6H1Q3W.
PhylomeDBiP10372.

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.

P10372-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIPALDLID GTVVRLHQGD YARQRDYGND PLPRLQDYAA QGAGVLHLVD
60 70 80 90 100
LTGAKDPAKR QIPLIKTLVA GVNVPVQVGG GVRTEEDVAA LLKAGVARVV
110 120 130 140 150
IGSTAVKSPD VVKGWFERFG AQALVLALDV RIDEHGTKQV AVSGWQENSG
160 170 180 190 200
VSLEQLVETY LPVGLKHVLC TDISRDGTLA GSNVSLYEEV CARYPQIAFQ
210 220 230 240
SSGGIGDIDD IAALRGTGVR GVIVGRALLE GKFTVKEAIQ CWQNV
Length:245
Mass (Da):26,089
Last modified:January 23, 2002 - v2
Checksum:i20CF123F43DCE925
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1242AL → GV in CAA31827 (PubMed:3062174).Curated
Sequence conflicti135 – 1351H → Q in CAA31827 (PubMed:3062174).Curated
Sequence conflicti177 – 1771G → A in CAA31827 (PubMed:3062174).Curated
Sequence conflicti211 – 2111I → DV (PubMed:3062174).Curated
Sequence conflicti222 – 2221V → M in CAA31827 (PubMed:3062174).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13464 Genomic DNA. Translation: CAA31827.1.
AE006468 Genomic DNA. Translation: AAL20980.1.
PIRiJS0161. ISEBIC.
RefSeqiNP_461021.1. NC_003197.1.
WP_000586409.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20980; AAL20980; STM2076.
GeneIDi1253597.
KEGGistm:STM2076.
PATRICi32382735. VBISalEnt20916_2198.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13464 Genomic DNA. Translation: CAA31827.1.
AE006468 Genomic DNA. Translation: AAL20980.1.
PIRiJS0161. ISEBIC.
RefSeqiNP_461021.1. NC_003197.1.
WP_000586409.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5A5WX-ray1.60A1-245[»]
5AHEX-ray1.70A1-245[»]
5AHFX-ray2.20A1-245[»]
5AHIX-ray2.00A1-245[»]
ProteinModelPortaliP10372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2076.

Proteomic databases

PaxDbiP10372.
PRIDEiP10372.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20980; AAL20980; STM2076.
GeneIDi1253597.
KEGGistm:STM2076.
PATRICi32382735. VBISalEnt20916_2198.

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
HOGENOMiHOG000224614.
KOiK01814.
OMAiEWLHLVD.
OrthoDBiEOG6H1Q3W.
PhylomeDBiP10372.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciSENT99287:GCTI-2088-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

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.

Entry informationi

Entry nameiHIS4_SALTY
AccessioniPrimary (citable) accession number: P10372
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2002
Last modified: April 13, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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.