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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)DescriptionActionsGraphical viewLength
Active sitei7Proton acceptorBy similarity1
Active sitei129Proton donorBy similarity1

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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001420491 – 2451-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST245

Proteomic databases

PaxDbiP10372.
PRIDEiP10372.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM2076.

Structurei

Secondary structure

1245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Beta strandi12 – 16Combined sources5
Helixi17 – 19Combined sources3
Beta strandi23 – 26Combined sources4
Helixi31 – 40Combined sources10
Beta strandi46 – 50Combined sources5
Helixi51 – 55Combined sources5
Helixi57 – 59Combined sources3
Helixi62 – 70Combined sources9
Beta strandi72 – 74Combined sources3
Beta strandi76 – 81Combined sources6
Helixi85 – 93Combined sources9
Beta strandi97 – 101Combined sources5
Helixi103 – 107Combined sources5
Helixi109 – 119Combined sources11
Helixi121 – 123Combined sources3
Beta strandi124 – 127Combined sources4
Beta strandi130 – 132Combined sources3
Beta strandi138 – 142Combined sources5
Turni143 – 146Combined sources4
Beta strandi147 – 152Combined sources6
Helixi153 – 160Combined sources8
Helixi161 – 163Combined sources3
Beta strandi167 – 172Combined sources6
Turni173 – 177Combined sources5
Helixi184 – 193Combined sources10
Beta strandi197 – 203Combined sources7
Helixi208 – 212Combined sources5
Turni213 – 217Combined sources5
Beta strandi220 – 224Combined sources5
Helixi226 – 229Combined sources4
Helixi235 – 244Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A5WX-ray1.60A1-245[»]
5AB3X-ray1.80A/B/C1-245[»]
5ABTX-ray1.65A1-245[»]
5AC6X-ray1.99A1-245[»]
5AC7X-ray1.90A/B1-245[»]
5AC8X-ray1.70A1-245[»]
5AHEX-ray1.70A1-245[»]
5AHFX-ray2.20A1-245[»]
5AHIX-ray2.00A1-245[»]
ProteinModelPortaliP10372.
SMRiP10372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

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

Family and domain databases

CDDicd04732. HisA. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti123 – 124AL → GV in CAA31827 (PubMed:3062174).Curated2
Sequence conflicti135H → Q in CAA31827 (PubMed:3062174).Curated1
Sequence conflicti177G → A in CAA31827 (PubMed:3062174).Curated1
Sequence conflicti211I → DV (PubMed:3062174).Curated1
Sequence conflicti222V → M in CAA31827 (PubMed:3062174).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A5WX-ray1.60A1-245[»]
5AB3X-ray1.80A/B/C1-245[»]
5ABTX-ray1.65A1-245[»]
5AC6X-ray1.99A1-245[»]
5AC7X-ray1.90A/B1-245[»]
5AC8X-ray1.70A1-245[»]
5AHEX-ray1.70A1-245[»]
5AHFX-ray2.20A1-245[»]
5AHIX-ray2.00A1-245[»]
ProteinModelPortaliP10372.
SMRiP10372.
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.
PhylomeDBiP10372.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.

Family and domain databases

CDDicd04732. HisA. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA. 1 hit.
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...

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: November 30, 2016
This is version 123 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.