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Q9X0C6

- HIS6_THEMA

UniProt

Q9X0C6 - HIS6_THEMA

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Protein

Imidazole glycerol phosphate synthase subunit HisF

Gene

hisF

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

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.

Kineticsi

  1. KM=1.5 µM for PRFAR1 Publication
  2. KM=2.2 mM for NH31 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Sequence Analysis
Active sitei130 – 1301Sequence Analysis

GO - Molecular functioni

  1. imidazoleglycerol-phosphate synthase activity Source: UniProtKB-HAMAP
  2. lyase activity Source: UniProtKB-KW

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-467.
UniPathwayiUPA00031; UER00010.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:hisF
Ordered Locus Names:TM_1036
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91C → A: No change in activity. 1 Publication
Mutagenesisi11 – 111D → X: Loss of activity. 1 Publication
Mutagenesisi19 – 191K → S: Decrease in activity. 1 Publication
Mutagenesisi51 – 511D → N: No change in activity. 1 Publication
Mutagenesisi103 – 1031N → A: No change in activity. 1 Publication
Mutagenesisi130 – 1301D → A, C, F, G, H, I, K, L, M, N, P, Q, R, S, T, V, W or Y: Complete loss of activity. 1 Publication
Mutagenesisi130 – 1301D → E: Weak activity. 1 Publication
Mutagenesisi176 – 1761D → N: Decrease in activity. 1 Publication
Mutagenesisi183 – 1831D → N: No change in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 253253Imidazole glycerol phosphate synthase subunit HisFPRO_0000142253Add
BLAST

Interactioni

Subunit structurei

Heterodimer of HisH and HisF.

Protein-protein interaction databases

DIPiDIP-59020N.
STRINGi243274.TM1036.

Structurei

Secondary structure

1
253
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi16 – 238Combined sources
Helixi32 – 4110Combined sources
Beta strandi46 – 538Combined sources
Beta strandi55 – 573Combined sources
Helixi58 – 7013Combined sources
Beta strandi77 – 826Combined sources
Helixi86 – 949Combined sources
Beta strandi98 – 1036Combined sources
Helixi104 – 1085Combined sources
Helixi111 – 12010Combined sources
Helixi122 – 1243Combined sources
Beta strandi125 – 13410Combined sources
Beta strandi137 – 1426Combined sources
Turni143 – 1464Combined sources
Beta strandi147 – 1526Combined sources
Helixi153 – 16210Combined sources
Beta strandi166 – 1727Combined sources
Turni173 – 1775Combined sources
Helixi184 – 1907Combined sources
Helixi191 – 1933Combined sources
Beta strandi198 – 2025Combined sources
Helixi207 – 2159Combined sources
Beta strandi219 – 2246Combined sources
Helixi225 – 2284Combined sources
Beta strandi229 – 2324Combined sources
Helixi234 – 24310Combined sources
Beta strandi250 – 2534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9X0C6.
SMRiQ9X0C6. Positions 1-251.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0C6.

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

eggNOGiCOG0107.
InParanoidiQ9X0C6.
KOiK02500.
OMAiDSYKVKQ.
OrthoDBiEOG6H1Q3W.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01013. HisF.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00735. hisF. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X0C6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL
60 70 80 90 100
DITASVEKRK TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV
110 120 130 140 150
SINTAAVENP SLITQIAQTF GSQAVVVAID AKRVDGEFMV FTYSGKKNTG
160 170 180 190 200
ILLRDWVVEV EKRGAGEILL TSIDRDGTKS GYDTEMIRFV RPLTTLPIIA
210 220 230 240 250
SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY LKKHGVNVRL

EGL
Length:253
Mass (Da):27,719
Last modified:November 1, 1999 - v1
Checksum:iFE0F97F0C57E9025
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36113.1.
PIRiC72304.
RefSeqiNP_228842.1. NC_000853.1.
YP_007977389.1. NC_021214.1.
YP_008991868.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36113; AAD36113; TM_1036.
GeneIDi18093682.
897046.
KEGGitma:TM1036.
PATRICi23937001. VBITheMar51294_1049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36113.1 .
PIRi C72304.
RefSeqi NP_228842.1. NC_000853.1.
YP_007977389.1. NC_021214.1.
YP_008991868.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GPW X-ray 2.40 A/C/E 1-253 [» ]
1THF X-ray 1.45 D 1-253 [» ]
1VH7 X-ray 1.90 A 2-253 [» ]
2A0N X-ray 1.64 A 1-253 [» ]
2LLE NMR - A 103-247 [» ]
2W6R X-ray 2.10 A 123-253 [» ]
2WJZ X-ray 2.60 A/C/E 1-253 [» ]
3CWO X-ray 3.10 X 103-253 [» ]
3OG3 X-ray 2.08 A 43-221 [» ]
3ZR4 X-ray 2.41 A/C/E 1-253 [» ]
4EWN X-ray 1.90 D 1-253 [» ]
4FX7 X-ray 2.08 A/B/C/D 99-219 [» ]
4J9J X-ray 2.30 A 91-220 [» ]
ProteinModelPortali Q9X0C6.
SMRi Q9X0C6. Positions 1-251.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59020N.
STRINGi 243274.TM1036.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36113 ; AAD36113 ; TM_1036 .
GeneIDi 18093682.
897046.
KEGGi tma:TM1036.
PATRICi 23937001. VBITheMar51294_1049.

Phylogenomic databases

eggNOGi COG0107.
InParanoidi Q9X0C6.
KOi K02500.
OMAi DSYKVKQ.
OrthoDBi EOG6H1Q3W.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00010 .
BioCyci MetaCyc:MONOMER-467.

Miscellaneous databases

EvolutionaryTracei Q9X0C6.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01013. HisF.
InterProi IPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR011060. RibuloseP-bd_barrel.
[Graphical view ]
Pfami PF00977. His_biosynth. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 1 hit.
TIGRFAMsi TIGR00735. hisF. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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).

Entry informationi

Entry nameiHIS6_THEMA
AccessioniPrimary (citable) accession number: Q9X0C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3