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Protein

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

Gene

hisA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 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.

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

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • histidine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:PRIBFAICARPISOM-MONOMER.
ECOL316407:JW2006-MONOMER.
MetaCyc:PRIBFAICARPISOM-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:b2024, JW2006
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10444. hisA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001420041 – 2451-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST245

Proteomic databases

EPDiP10371.
PaxDbiP10371.
PRIDEiP10371.

2D gel databases

SWISS-2DPAGEP10371.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4260420. 26 interactors.
IntActiP10371. 3 interactors.
STRINGi511145.b2024.

Structurei

3D structure databases

ProteinModelPortaliP10371.
SMRiP10371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
HOGENOMiHOG000224614.
InParanoidiP10371.
KOiK01814.
OMAiEWLHLVD.
PhylomeDBiP10371.

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.

P10371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIPALDLID GTVVRLHQGD YGKQRDYGND PLPRLQDYAA QGAEVLHLVD
60 70 80 90 100
LTGAKDPAKR QIPLIKTLVA GVNVPVQVGG GVRSEEDVAA LLEAGVARVV
110 120 130 140 150
VGSTAVKSQD MVKGWFERFG ADALVLALDV RIDEQGNKQV AVSGWQENSG
160 170 180 190 200
VSLEQLVETY LPVGLKHVLC TDISRDGTLA GSNVSLYEEV CARYPQVAFQ
210 220 230 240
SSGGIGDIDD VAALRGTGVR GVIVGRALLE GKFTVKEAIA CWQNA
Length:245
Mass (Da):26,033
Last modified:November 1, 1997 - v2
Checksum:iB21D590E4214EE7E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84S → T in CAA31816 (PubMed:3062174).Curated1
Sequence conflicti126L → V in CAA31816 (PubMed:3062174).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31816.1.
U00096 Genomic DNA. Translation: AAC75085.2.
AP009048 Genomic DNA. Translation: BAA15855.1.
PIRiG64967. ISECIC.
RefSeqiNP_416528.2. NC_000913.3.
WP_000586462.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75085; AAC75085; b2024.
BAA15855; BAA15855; BAA15855.
GeneIDi946521.
KEGGiecj:JW2006.
eco:b2024.
PATRICi32119383. VBIEscCol129921_2101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13462 Genomic DNA. Translation: CAA31816.1.
U00096 Genomic DNA. Translation: AAC75085.2.
AP009048 Genomic DNA. Translation: BAA15855.1.
PIRiG64967. ISECIC.
RefSeqiNP_416528.2. NC_000913.3.
WP_000586462.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP10371.
SMRiP10371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260420. 26 interactors.
IntActiP10371. 3 interactors.
STRINGi511145.b2024.

2D gel databases

SWISS-2DPAGEP10371.

Proteomic databases

EPDiP10371.
PaxDbiP10371.
PRIDEiP10371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75085; AAC75085; b2024.
BAA15855; BAA15855; BAA15855.
GeneIDi946521.
KEGGiecj:JW2006.
eco:b2024.
PATRICi32119383. VBIEscCol129921_2101.

Organism-specific databases

EchoBASEiEB0439.
EcoGeneiEG10444. hisA.

Phylogenomic databases

eggNOGiENOG4105CJV. Bacteria.
COG0106. LUCA.
HOGENOMiHOG000224614.
InParanoidiP10371.
KOiK01814.
OMAiEWLHLVD.
PhylomeDBiP10371.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciEcoCyc:PRIBFAICARPISOM-MONOMER.
ECOL316407:JW2006-MONOMER.
MetaCyc:PRIBFAICARPISOM-MONOMER.

Miscellaneous databases

PROiP10371.

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_ECOLI
AccessioniPrimary (citable) accession number: P10371
Secondary accession number(s): P78078
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.