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A5INE5 (HIS4_THEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:hisA
Ordered Locus Names:Tpet_1713
OrganismThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP]
Taxonomic identifier390874 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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. HAMAP-Rule MF_01014

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01014.

Sequence similarities

Belongs to the HisA/HisF family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processhistidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2412411-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_1000063240

Sites

Active site81Proton acceptor By similarity
Active site1271Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
A5INE5 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 7DE09FB4DE200FED

FASTA24127,259
        10         20         30         40         50         60 
MLVVPAIDLF RGKVARMVKG KKENTIFYEK DPAELVKKLI EEGFTLIHVV DLSKAIENSV 

        70         80         90        100        110        120 
ENFPVLERLS EFAEHIQIGG GIRSFDYAER LRKLGYKRQI VSSKVLEDPS FLKFLKEIDV 

       130        140        150        160        170        180 
EPVFSLDTRG GKVAFKGWLA EEEIDPISLL KRLKEYGLEE IVHTEIEKDG TLQEHDFSLT 

       190        200        210        220        230        240 
RKIAIEAEVN VFAAGGISSE NSLKTAQRVH RETNGLLKGV IVGRAFLEGI LTVEVMKRYA 


R 

« Hide

References

[1]"Complete sequence of Thermotoga petrophila RKU-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000702 Genomic DNA. Translation: ABQ47718.1.
RefSeqYP_001245294.1. NC_009486.1.

3D structure databases

ProteinModelPortalA5INE5.
SMRA5INE5. Positions 1-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390874.Tpet_1713.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ47718; ABQ47718; Tpet_1713.
GeneID5171639.
KEGGtpt:Tpet_1713.
PATRIC23946281. VBIThePet65348_1733.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAKKENTIF.
OrthoDBEOG6H1Q3W.

Enzyme and pathway databases

BioCycTPET390874:GHJI-1764-MONOMER.
UniPathwayUPA00031; UER00009.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01014. HisA.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00007. TIGR00007. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS4_THEP1
AccessionPrimary (citable) accession number: A5INE5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 26, 2007
Last modified: May 14, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways