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Q2FN18 (HIS4_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:Mhun_0921
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length236 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
Reference 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 – 2362361-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP-Rule MF_01014
PRO_0000290578

Sites

Active site81Proton acceptor By similarity
Active site1291Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FN18 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 097C36232796409D

FASTA23624,876
        10         20         30         40         50         60 
MIVFPAVDIL GGRCVQLVQG KRETATSYGD PLLCAESWIN QGAEALHIVN LDGAFGSSKL 

        70         80         90        100        110        120 
NAEKITDVII RTGVKTQLGG GIRSLDDARS WLDCGVDRII ISTFAADDPE CLTILSEEYG 

       130        140        150        160        170        180 
SDRIMAGVDA RAGEMVTHGW ERPAGDFLEW ADLFIRKGAG SLLYTNVSVE GLCNGIDPKP 

       190        200        210        220        230 
IRDLLSTVSV PVVVAGGITS PSDIKILKEA DAAGVVLGSA LYSGKITLQE ALEAAG 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD40671.1.
RefSeqYP_502390.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FN18.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_0921.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD40671; ABD40671; Mhun_0921.
GeneID3924608.
KEGGmhu:Mhun_0921.

Phylogenomic databases

eggNOGCOG0106.
HOGENOMHOG000224614.
KOK01814.
OMACARYVVT.
ProtClustDBPRK13585.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-938-MONOMER.
UniPathwayUPA00031; UER00009.

Family and domain databases

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

Entry information

Entry nameHIS4_METHJ
AccessionPrimary (citable) accession number: Q2FN18
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 51 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