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Q9X0C6 (HIS6_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
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:TM_1036
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length253 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. 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.

Subcellular location

Cytoplasm HAMAP-Rule MF_01013.

Sequence similarities

Belongs to the HisA/HisF family.

Biophysicochemical properties

Kinetic parameters:

KM=1.5 µM for PRFAR Ref.2

KM=2.2 mM for NH3

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Histidine biosynthesis
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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_functionimidazoleglycerol-phosphate synthase activity

Inferred from electronic annotation. Source: UniProtKB-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 – 253253Imidazole glycerol phosphate synthase subunit HisF HAMAP-Rule MF_01013
PRO_0000142253

Sites

Active site111 Potential
Active site1301 Potential

Experimental info

Mutagenesis91C → A: No change in activity. Ref.2
Mutagenesis111D → X: Loss of activity. Ref.2
Mutagenesis191K → S: Decrease in activity. Ref.2
Mutagenesis511D → N: No change in activity. Ref.2
Mutagenesis1031N → A: No change in activity. Ref.2
Mutagenesis1301D → A, C, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Complete loss of activity. Ref.2
Mutagenesis1301D → E: Weak activity. Ref.2
Mutagenesis1761D → N: Decrease in activity. Ref.2
Mutagenesis1831D → N: No change in activity. Ref.2

Secondary structure

.............................................. 253
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X0C6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: FE0F97F0C57E9025

FASTA25327,719
        10         20         30         40         50         60 
MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL DITASVEKRK 

        70         80         90        100        110        120 
TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV SINTAAVENP SLITQIAQTF 

       130        140        150        160        170        180 
GSQAVVVAID AKRVDGEFMV FTYSGKKNTG ILLRDWVVEV EKRGAGEILL TSIDRDGTKS 

       190        200        210        220        230        240 
GYDTEMIRFV RPLTTLPIIA SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY 

       250 
LKKHGVNVRL EGL 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex."
Beismann-Driemeyer S., Sterner R.
J. Biol. Chem. 276:20387-20396(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF CYS-9; ASP-11; LYS-19; ASP-51; ASN-103; ASP-130; ASP-176 AND ASP-183, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM.
[3]"Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion."
Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.
Science 289:1546-1550(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[4]"Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex."
Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., Sterner R., Wilmanns M.
Structure 10:185-193(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36113.1.
PIRC72304.
RefSeqNP_228842.1. NC_000853.1.
YP_007977389.1. NC_021214.1.
YP_008991868.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPWX-ray2.40A/C/E1-253[»]
1THFX-ray1.45D1-253[»]
1VH7X-ray1.90A2-253[»]
2A0NX-ray1.64A1-253[»]
2LLENMR-A103-247[»]
2W6RX-ray2.10A123-253[»]
2WJZX-ray2.60A/C/E1-253[»]
3CWOX-ray3.10X103-253[»]
3OG3X-ray2.08A43-221[»]
3ZR4X-ray2.41A/C/E1-253[»]
4EWNX-ray1.90D1-253[»]
4FX7X-ray2.08A/B/C/D99-219[»]
4J9JX-ray2.30A91-220[»]
ProteinModelPortalQ9X0C6.
SMRQ9X0C6. Positions 1-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59020N.
STRING243274.TM1036.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD36113; AAD36113; TM_1036.
GeneID897046.
KEGGtma:TM1036.
tmi:THEMA_09180.
tmm:Tmari_1040.
PATRIC23937001. VBITheMar51294_1049.

Phylogenomic databases

eggNOGCOG0107.
KOK02500.
OMADSYKVKQ.
OrthoDBEOG6H1Q3W.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-467.
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. SSF51366. 1 hit.
TIGRFAMsTIGR00735. hisF. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9X0C6.

Entry information

Entry nameHIS6_THEMA
AccessionPrimary (citable) accession number: Q9X0C6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 106 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways