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Q3SEU7 (HIS4_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:Tbd_1709
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length251 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 – 2512511-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000229090

Sites

Active site81Proton acceptor By similarity
Active site1311Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SEU7 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 1702704D0FA02565

FASTA25126,503
        10         20         30         40         50         60 
MLIIPAIDLK DGHCVRLEQG EMDKATVFSE DPAAMARRWK EHGARRLHLV DLNGAFAGKP 

        70         80         90        100        110        120 
VNDAAIQAIV EAVGDEMPVQ LGGGIRDLAT IERYLDDGVR YVIIGTAAVK NPGFLHEACD 

       130        140        150        160        170        180 
AFPGHVMVGL DARDGKVAVE GWSKLTGHDV VDLAKRFEGY GVEAVIYTDI GRDGMLTGVN 

       190        200        210        220        230        240 
IDATQRLAQA LSIPVIASGG VTNLDDVRGL SAVAKDGIIG AITGRAIYQG TLDFAEAQKL 

       250 
ADELAGGVFG V 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ97662.1.
RefSeqYP_315467.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SEU7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_1709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ97662; AAZ97662; Tbd_1709.
GeneID3671292.
KEGGtbd:Tbd_1709.
PATRIC23969579. VBIThiDen82923_1692.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMAGWAEETD.
OrthoDBEOG6H1Q3W.

Enzyme and pathway databases

BioCycTDEN292415:GHWG-1743-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_THIDA
AccessionPrimary (citable) accession number: Q3SEU7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2005
Last modified: May 14, 2014
This is version 62 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