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
Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
Status
Reviewed-Annotation score: -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: 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. Imidazoleglycerol phosphate synthase, cyclase subunit (hisF-1), Imidazole glycerol phosphate synthase subunit HisH (hisH-1), 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)DescriptionActionsGraphical viewLength
Active sitei9Proton acceptorUniRule annotation1
Active sitei131Proton donorUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processAmino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciCJEJ360109:G1G9I-1825-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:JJD26997_1956
OrganismiCampylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
Taxonomic identifieri360109 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000002302 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000631991 – 2441-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST244

Structurei

3D structure databases

ProteinModelPortaliA7H5V3
SMRiA7H5V3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000224614
KOiK01814
OMAiEWLHLVD
OrthoDBiPOG091H048O

Family and domain databases

CDDicd04732 HisA, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01014 HisA, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006062 His_biosynth
IPR006063 HisA
IPR023016 Isoase_HisA
IPR011060 RibuloseP-bd_barrel
PfamiView protein in Pfam
PF00977 His_biosynth, 1 hit
SUPFAMiSSF51366 SSF51366, 1 hit
TIGRFAMsiTIGR00007 TIGR00007, 1 hit

Sequencei

Sequence statusi: Complete.

A7H5V3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQIIPALDL IDGEVVRLVK GDYKQKKVYK YNPLKKFKEY EKAGAKELHL
60 70 80 90 100
VDLTGAKDPS KRQLVLIEKL AKEVSVNLQV GGGIRSKEEV KALLDCGVKR
110 120 130 140 150
VVIGSMAIKD ATLCLEILKK FGSEAIVLAL DTILKEDYVV AVNAWQEASD
160 170 180 190 200
KKLMEVLDFY SNKGLKHILC TDISKDGTMQ GVNVRLYKLI HEIFPKICIQ
210 220 230 240
ASGGVASLKD LENLKGICSG VIVGKALLDG VFSVEEGIRC LQNA
Length:244
Mass (Da):26,819
Last modified:September 11, 2007 - v1
Checksum:i8E1354F07F47C2A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000768 Genomic DNA Translation: ABS43305.1

Genome annotation databases

EnsemblBacteriaiABS43305; ABS43305; JJD26997_1956
KEGGicjd:JJD26997_1956

Similar proteinsi

Entry informationi

Entry nameiHIS4_CAMJD
AccessioniPrimary (citable) accession number: A7H5V3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 11, 2007
Last modified: March 28, 2018
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health