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Protein

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

Gene

hisA

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
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 hisF1 (hisF1), Imidazole glycerol phosphate synthase subunit HisH 2 (hisH2), Imidazole glycerol phosphate synthase subunit HisH 1 (hisH1), Putative imidazole glycerol phosphate synthase subunit hisF2 (hisF2)
  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 acceptorBy similarity1
Active sitei131Proton 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

BioCyciCJEJ192222:GJTS-1502-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:Cj1601
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001419931 – 2431-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST243

Proteomic databases

PaxDbiQ9PM74.

Interactioni

Protein-protein interaction databases

STRINGi192222.Cj1601.

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi14 – 19Combined sources6
Beta strandi21 – 23Combined sources3
Beta strandi25 – 28Combined sources4
Helixi33 – 43Combined sources11
Beta strandi47 – 52Combined sources6
Helixi53 – 57Combined sources5
Helixi59 – 61Combined sources3
Helixi64 – 73Combined sources10
Beta strandi76 – 83Combined sources8
Helixi87 – 95Combined sources9
Beta strandi99 – 103Combined sources5
Turni105 – 109Combined sources5
Helixi111 – 121Combined sources11
Turni123 – 125Combined sources3
Beta strandi126 – 140Combined sources15
Helixi153 – 161Combined sources9
Turni162 – 164Combined sources3
Beta strandi167 – 172Combined sources6
Helixi184 – 193Combined sources10
Beta strandi197 – 203Combined sources7
Helixi208 – 213Combined sources6
Turni214 – 217Combined sources4
Beta strandi219 – 223Combined sources5
Helixi225 – 228Combined sources4
Helixi234 – 241Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GJ1X-ray2.15A1-243[»]
ProteinModelPortaliQ9PM74.
SMRiQ9PM74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

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

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.

Q9PM74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQIIPALDL IDGEVVRLVK GDYEQKKVYK YNPLKKFKEY EKAGAKELHL
60 70 80 90 100
VDLTGAKDPS KRQFALIEKL AKEVSVNLQV GGGIRSKEEV KALLDCGVKR
110 120 130 140 150
VVIGSMAIKD ATLCLEILKE FGSEAIVLAL DTILKEDYVV AVNAWQEASD
160 170 180 190 200
KKLMEVLDFY SNKGLKHILC TDISKDGTMQ GVNVRLYKLI HEIFPNICIQ
210 220 230 240
ASGGVASLKD LENLKGICSG VIVGKALLDG VFSVEEGIRC LAN
Length:243
Mass (Da):26,684
Last modified:October 1, 2000 - v1
Checksum:i23AE7D77A2ECD9A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35698.1.
PIRiG81255.
RefSeqiWP_002851391.1. NC_002163.1.
YP_002344970.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35698; CAL35698; Cj1601.
GeneIDi904505.
KEGGicje:Cj1601.
PATRICi20060162. VBICamJej33762_1577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35698.1.
PIRiG81255.
RefSeqiWP_002851391.1. NC_002163.1.
YP_002344970.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GJ1X-ray2.15A1-243[»]
ProteinModelPortaliQ9PM74.
SMRiQ9PM74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192222.Cj1601.

Proteomic databases

PaxDbiQ9PM74.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL35698; CAL35698; Cj1601.
GeneIDi904505.
KEGGicje:Cj1601.
PATRICi20060162. VBICamJej33762_1577.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciCJEJ192222:GJTS-1502-MONOMER.

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_CAMJE
AccessioniPrimary (citable) accession number: Q9PM74
Secondary accession number(s): Q0P827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 99 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

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.