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P05324 (HIS4_METVA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. 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
OrganismMethanococcus vannielii
Taxonomic identifier2187 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Protein attributes

Sequence length238 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
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 – 2382381-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000142098

Sites

Active site81Proton acceptor By similarity
Active site1301Proton donor By similarity

Experimental info

Sequence conflict261H → Q in CAA30300. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P05324 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 5082D2AF54D9E756

FASTA23825,712
        10         20         30         40         50         60 
MLIIPAVDMK NKKCVQLIQG NPDKKHVELD NPPEIAKKWV EQGAEMLHLV NLDGAINGKR 

        70         80         90        100        110        120 
VNDEFIEETI KNSGVPVQIG GGIRSVSDAL YFIEKGAEKV ILGTVAIQNP KIVREISSIV 

       130        140        150        160        170        180 
GKEKVTVALD AKDGKVLIKG WTEKTDYSPV QIGKILENMG AGSILFTNVD SEGLLEGINV 

       190        200        210        220        230 
LPTKELVDNL NIPIIASGGV TTVEDLLKFK EIGVYAVVVG SALYKDMINL KDAILASK 

« Hide

References

[1]"Structure and sequence divergence of two archaebacterial genes."
Cue D., Beckler G.S., Reeve J.N., Konisky J.
Proc. Natl. Acad. Sci. U.S.A. 82:4207-4211(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"An archaebacterial RNA polymerase binding site and transcription initiation of the hisA gene in Methanococcus vannielii."
Brown J.W., Thomm M., Beckler G.S., Frey G., Stetter K.O., Reeve J.N.
Nucleic Acids Res. 16:135-150(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11219 Genomic DNA. Translation: AAA72490.1.
X07391 Genomic DNA. Translation: CAA30300.1.
PIRS00580.
T48888.

3D structure databases

ProteinModelPortalP05324.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_METVA
AccessionPrimary (citable) accession number: P05324
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: February 19, 2014
This is version 84 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