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
Thiomicrospira crunogena (strain XCL-2)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  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 sitei8 – 81Proton acceptorUniRule annotation
Active sitei130 – 1301Proton 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

BioCyciTCRU317025:GHE8-2024-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:Tcr_1968
OrganismiThiomicrospira crunogena (strain XCL-2)
Taxonomic identifieri317025 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira
ProteomesiUP000002713 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 – 2462461-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000229091Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi317025.Tcr_1968.

Structurei

3D structure databases

ProteinModelPortaliQ31E65.
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.
IPR001252. Malate_DH_AS.
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.

Q31E65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLIPAIDLK DGECVRLRQG LMDDATVFSG DIVAMAERWV NQGARRLHMV
60 70 80 90 100
DLNGAFEGKP VNGDAVYQVR EAFPDLPIQI GGGIRDLETI EAYLKAGVSY
110 120 130 140 150
CIIGTKAVHN PEFVAEACKA FPGHIMVGLD AKEGMVAING WAEVTDHNVI
160 170 180 190 200
DLGKQFENDG VEAIIYTDIG RDGMMQGVNI QATQALAKAL NIPIIASGGI
210 220 230 240
TNLDDIRALA TIEKDGVSGA ITGRAIYEGS LNFKEGQALS DELSKA
Length:246
Mass (Da):26,285
Last modified:December 6, 2005 - v1
Checksum:iCF2D54198867D52C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000109 Genomic DNA. Translation: ABB42558.1.
RefSeqiWP_011371385.1. NC_007520.2.

Genome annotation databases

EnsemblBacteriaiABB42558; ABB42558; Tcr_1968.
KEGGitcx:Tcr_1968.
PATRICi23976060. VBIThiCru83387_2052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000109 Genomic DNA. Translation: ABB42558.1.
RefSeqiWP_011371385.1. NC_007520.2.

3D structure databases

ProteinModelPortaliQ31E65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi317025.Tcr_1968.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB42558; ABB42558; Tcr_1968.
KEGGitcx:Tcr_1968.
PATRICi23976060. VBIThiCru83387_2052.

Phylogenomic databases

eggNOGiCOG0106.
HOGENOMiHOG000224614.
KOiK01814.
OMAiHCVRLKQ.
OrthoDBiEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.
BioCyciTCRU317025:GHE8-2024-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.
IPR001252. Malate_DH_AS.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00007. TIGR00007. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: XCL-2.

Entry informationi

Entry nameiHIS4_THICR
AccessioniPrimary (citable) accession number: Q31E65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 6, 2005
Last modified: May 27, 2015
This is version 66 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, Reference 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.