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Q9X0C6

- HIS6_THEMA

UniProt

Q9X0C6 - HIS6_THEMA

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Protein
Imidazole glycerol phosphate synthase subunit HisF
Gene
hisF, TM_1036
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.UniRule annotation

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.UniRule annotation

Kineticsi

  1. KM=1.5 µM for PRFAR1 Publication
  2. KM=2.2 mM for NH3

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111 Reviewed prediction
Active sitei130 – 1301 Reviewed prediction

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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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 HisFUniRule annotation
PRO_0000142253Add
BLAST

Interactioni

Subunit structurei

Heterodimer of HisH and HisF.

Protein-protein interaction databases

DIPiDIP-59020N.
STRINGi243274.TM1036.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiQ9X0C6.

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.

Phylogenomic databases

eggNOGiCOG0107.
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

MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL    50
DITASVEKRK TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV 100
SINTAAVENP SLITQIAQTF GSQAVVVAID AKRVDGEFMV FTYSGKKNTG 150
ILLRDWVVEV EKRGAGEILL TSIDRDGTKS GYDTEMIRFV RPLTTLPIIA 200
SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY LKKHGVNVRL 250
EGL 253
Length:253
Mass (Da):27,719
Last modified:November 1, 1999 - v1
Checksum:iFE0F97F0C57E9025
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi897046.
KEGGitma:TM1036.
tmi:THEMA_09180.
tmm:Tmari_1040.
PATRICi23937001. VBITheMar51294_1049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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 897046.
KEGGi tma:TM1036.
tmi:THEMA_09180.
tmm:Tmari_1040.
PATRICi 23937001. VBITheMar51294_1049.

Phylogenomic databases

eggNOGi COG0107.
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: July 9, 2014
This is version 106 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

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