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Q1H4R2 (HIS6_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Imidazole glycerol phosphate synthase subunit HisF

EC=4.1.3.-
Alternative name(s):
IGP synthase cyclase subunit
IGP synthase subunit HisF
ImGP synthase subunit HisF
Short name=IGPS subunit HisF
Gene names
Name:hisF
Ordered Locus Names:Mfla_0254
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit By similarity. HAMAP-Rule MF_01013

Catalytic activity

5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide + L-glutamine = imidazole-glycerol phosphate + 5-aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H2O. HAMAP-Rule MF_01013

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. HAMAP-Rule MF_01013

Subunit structure

Heterodimer of HisH and HisF By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the HisA/HisF family.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionimidazoleglycerol-phosphate synthase activity

Inferred from electronic annotation. Source: HAMAP

lyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Imidazole glycerol phosphate synthase subunit HisF HAMAP-Rule MF_01013
PRO_0000319460

Sites

Active site121 Potential
Active site1311 Potential

Sequences

Sequence LengthMass (Da)Tools
Q1H4R2 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 79163930FA6BF007

FASTA25227,056
        10         20         30         40         50         60 
MSLAKRIIPC LDVTNGRVVK GVNFLELRDA GDPVEIARRY DEQGADELTF LDITASSDNR 

        70         80         90        100        110        120 
GLMLGIIEQV ASQVFIPLTV GGGVREVEDI RRLLNAGADK VSINTAAVTN PQLVADAASR 

       130        140        150        160        170        180 
FGSQCIVVAI DAKQVGDHWE IFTHGGRTPT GLNAVDWARK MVELGAGELL VTSMDRDGTK 

       190        200        210        220        230        240 
MGFNLPLNRA ISEAVDVPII ASGGVGNLVH LVEGVREGGA DAVLAASIFH YGEYTVRQAK 

       250 
EYMRDQGIEV RL 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000284 Genomic DNA. Translation: ABE48525.1.
RefSeqYP_544366.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1H4R2.
SMRQ1H4R2. Positions 2-252.
ModBaseSearch...

Protein-protein interaction databases

STRING265072.Mfla_0254.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE48525; ABE48525; Mfla_0254.
GeneID3999074.
KEGGmfa:Mfla_0254.
PATRIC32266023. VBIMetFla97085_0259.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0107.
HOGENOMHOG000224612.
KOK02500.
OMARVVKGTN.
ProtClustDBCLSK2529135.

Enzyme and pathway databases

BioCycMFLA265072:GHWJ-317-MONOMER.
UniPathwayUPA00031; UER00010.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01013. HisF.
InterProIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMSSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR00735. hisF. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHIS6_METFK
AccessionPrimary (citable) accession number: Q1H4R2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 27, 2006
Last modified: May 1, 2013
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families