Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

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

Gene

hisA

Organism
Escherichia coli (strain UTI89 / UPEC)
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: 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.UniRule annotation
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  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 acceptorUniRule annotation
Active sitei129 – 1291Proton 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

BioCyciECOL364106:GHPQ-2279-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:UTI89_C2297
OrganismiEscherichia coli (strain UTI89 / UPEC)
Taxonomic identifieri364106 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001952 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 – 2452451-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000290472Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ1RA49.
SMRiQ1RA49. Positions 2-242.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiHCVRLKQ.
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.

Q1RA49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIPALDLID GTVVRLHQGD YGKQRDYGNN PLPRLQDYAA QGAEVLHLVD
60 70 80 90 100
LTGAKDPAKR QIPLIKTLVA GVNVPVQVGG GVRSEKDVAA LLEAGVARVV
110 120 130 140 150
VGSTAVKSPE MVKGWFERFG ADALVLALDV RIDEQGNKQV AVSGWQENSG
160 170 180 190 200
VSLEQLVETY LPVGLKHVLC TDISRDGTLA GSNVSLYEEV CARYPQVAFQ
210 220 230 240
SSGGIGDIND VAALRGTGVR GVIVGRALLE GKFTVKEAIA CWQNA
Length:245
Mass (Da):26,013
Last modified:June 12, 2007 - v2
Checksum:i21C8D381C819A8F0
GO

Sequence cautioni

The sequence ABE07765.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA. Translation: ABE07765.1. Different initiation.
RefSeqiWP_011478215.1. NC_007946.1.
YP_541296.1. NC_007946.1.

Genome annotation databases

EnsemblBacteriaiABE07765; ABE07765; UTI89_C2297.
KEGGieci:UTI89_C2297.
PATRICi18454174. VBIEscCol42261_2325.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000243 Genomic DNA. Translation: ABE07765.1. Different initiation.
RefSeqiWP_011478215.1. NC_007946.1.
YP_541296.1. NC_007946.1.

3D structure databases

ProteinModelPortaliQ1RA49.
SMRiQ1RA49. Positions 2-242.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE07765; ABE07765; UTI89_C2297.
KEGGieci:UTI89_C2297.
PATRICi18454174. VBIEscCol42261_2325.

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiHCVRLKQ.
OrthoDBiEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciECOL364106:GHPQ-2279-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. "Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
    Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
    Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UTI89 / UPEC.

Entry informationi

Entry nameiHIS4_ECOUT
AccessioniPrimary (citable) accession number: Q1RA49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: June 12, 2007
Last modified: June 24, 2015
This is version 59 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

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.