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Protein

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

Gene

hisA

Organism
Methanococcus vannielii
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.

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.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. no protein annotated in this organism
  8. no protein annotated in this organism
  9. no protein annotated in this organism
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 acceptorBy similarity
Active sitei130 – 1301Proton donorBy similarity

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

UniPathwayiUPA00031; UER00009.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:hisA
OrganismiMethanococcus vannielii
Taxonomic identifieri2187 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2382381-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000142098Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi406327.Mevan_1405.

Structurei

3D structure databases

ProteinModelPortaliP05324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
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.

P05324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLIIPAVDMK NKKCVQLIQG NPDKKHVELD NPPEIAKKWV EQGAEMLHLV
60 70 80 90 100
NLDGAINGKR VNDEFIEETI KNSGVPVQIG GGIRSVSDAL YFIEKGAEKV
110 120 130 140 150
ILGTVAIQNP KIVREISSIV GKEKVTVALD AKDGKVLIKG WTEKTDYSPV
160 170 180 190 200
QIGKILENMG AGSILFTNVD SEGLLEGINV LPTKELVDNL NIPIIASGGV
210 220 230
TTVEDLLKFK EIGVYAVVVG SALYKDMINL KDAILASK
Length:238
Mass (Da):25,712
Last modified:November 1, 1988 - v1
Checksum:i5082D2AF54D9E756
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261H → Q in CAA30300 (PubMed:2829115).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11219 Genomic DNA. Translation: AAA72490.1.
X07391 Genomic DNA. Translation: CAA30300.1.
PIRiS00580.
T48888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11219 Genomic DNA. Translation: AAA72490.1.
X07391 Genomic DNA. Translation: CAA30300.1.
PIRiS00580.
T48888.

3D structure databases

ProteinModelPortaliP05324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi406327.Mevan_1405.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00007. TIGR00007. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiHIS4_METVA
AccessioniPrimary (citable) accession number: P05324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: June 24, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.