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Protein

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

Gene

hisA

Organism
Escherichia coli O9:H4 (strain HS)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei7 – 71Proton acceptorUniRule annotation
Active sitei129 – 1291Proton donorUniRule annotation

GO - Molecular functioni

  1. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciECOL331112:GHHI-2149-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:EcHS_A2163
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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_1000063205Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi331112.EcHS_A2163.

Structurei

3D structure databases

ProteinModelPortaliA8A1P8.
SMRiA8A1P8. 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.

A8A1P8-1 [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
VGSTAVKSPE 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):26,016
Last modified:October 23, 2007 - v1
Checksum:i2CF26D4B4215AA3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV06452.1.
RefSeqiYP_001458835.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV06452; ABV06452; EcHS_A2163.
GeneIDi5591218.
KEGGiecx:EcHS_A2163.
PATRICi18314305. VBIEscCol77814_2116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV06452.1.
RefSeqiYP_001458835.1. NC_009800.1.

3D structure databases

ProteinModelPortaliA8A1P8.
SMRiA8A1P8. Positions 2-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi331112.EcHS_A2163.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV06452; ABV06452; EcHS_A2163.
GeneIDi5591218.
KEGGiecx:EcHS_A2163.
PATRICi18314305. VBIEscCol77814_2116.

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiHCVRLKQ.
OrthoDBiEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciECOL331112:GHHI-2149-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. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiHIS4_ECOHS
AccessioniPrimary (citable) accession number: A8A1P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 7, 2015
This is version 45 of the entry and version 1 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.