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Protein

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

Gene

hisA

Organism
Arthrobacter aurescens (strain TC1)
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.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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (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. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  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 sitei16 – 161Proton acceptorUniRule annotation
Active sitei135 – 1351Proton 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

BioCyciAAUR290340:GI59-1608-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:AAur_1608
OrganismiArthrobacter aurescens (strain TC1)
Taxonomic identifieri290340 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter
ProteomesiUP000000637 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 – 2472471-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000290447Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi290340.AAur_1608.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 189Combined sources
Beta strandi21 – 255Combined sources
Beta strandi34 – 374Combined sources
Helixi39 – 4810Combined sources
Beta strandi52 – 587Combined sources
Helixi59 – 624Combined sources
Helixi69 – 7810Combined sources
Beta strandi80 – 889Combined sources
Helixi92 – 1009Combined sources
Beta strandi104 – 1085Combined sources
Helixi110 – 1145Combined sources
Helixi116 – 12611Combined sources
Helixi127 – 1293Combined sources
Beta strandi130 – 1378Combined sources
Helixi153 – 16311Combined sources
Beta strandi168 – 1725Combined sources
Helixi184 – 19411Combined sources
Beta strandi198 – 2025Combined sources
Helixi207 – 2148Combined sources
Helixi215 – 2195Combined sources
Beta strandi221 – 2266Combined sources
Helixi228 – 2314Combined sources
Helixi237 – 2448Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WD0X-ray1.50A1-247[»]
ProteinModelPortaliA1R562.
SMRiA1R562. Positions 7-242.
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.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.

Sequencei

Sequence statusi: Complete.

A1R562-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSAQSVLE LLPAVDIVDG QAVRLLQGEA GSETSYGTPL EAALNWQNDG
60 70 80 90 100
AEWVHMVDLD AAFGRGNNAA LISDVVSQLN VKVELSGGLR DDESLERALE
110 120 130 140 150
LGVARVNLGT AALENPEWTR KAIDRFGDKI AVGLDVRGTT LAGRGWTKEG
160 170 180 190 200
GDLWEVLARL EDAGCARYVV TDVTKDGTLQ GPNVELLRQM VEKTGKPVVA
210 220 230 240
SGGISSLEDL RVLRELVPLG VEGAIVGKAL YAGAFTLPEA LDVAGRR
Length:247
Mass (Da):26,175
Last modified:February 6, 2007 - v1
Checksum:iA0839617E7505388
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000474 Genomic DNA. Translation: ABM09313.1.
RefSeqiWP_011774319.1. NC_008711.1.
YP_947374.1. NC_008711.1.

Genome annotation databases

EnsemblBacteriaiABM09313; ABM09313; AAur_1608.
KEGGiaau:AAur_1608.
PATRICi20978606. VBIArtAur67810_1640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000474 Genomic DNA. Translation: ABM09313.1.
RefSeqiWP_011774319.1. NC_008711.1.
YP_947374.1. NC_008711.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WD0X-ray1.50A1-247[»]
ProteinModelPortaliA1R562.
SMRiA1R562. Positions 7-242.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290340.AAur_1608.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM09313; ABM09313; AAur_1608.
KEGGiaau:AAur_1608.
PATRICi20978606. VBIArtAur67810_1640.

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiHCVRLKQ.
OrthoDBiEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciAAUR290340:GI59-1608-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR010188. HisA_TrpF.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01919. hisA-trpF. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TC1.

Entry informationi

Entry nameiHIS4_ARTAT
AccessioniPrimary (citable) accession number: A1R562
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: February 6, 2007
Last modified: June 24, 2015
This is version 58 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

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.