Q9X0C6 (HIS6_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	hisF
Ordered Locus Names:	TM_1036

Organism

Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]

Taxonomic identifier

243274 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima

Protein attributes

Sequence length	253 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	imidazoleglycerol-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 253

253

Imidazole glycerol phosphate synthase subunit HisF HAMAP-Rule MF_01013

PRO_0000142253

Sites

Active site

11

1

Potential

Active site

130

1

Potential

Experimental info

Mutagenesis

9

1

C → A: No change in activity. Ref.2

Mutagenesis

11

1

D → X: Loss of activity. Ref.2

Mutagenesis

19

1

K → S: Decrease in activity. Ref.2

Mutagenesis

51

1

D → N: No change in activity. Ref.2

Mutagenesis

103

1

N → A: No change in activity. Ref.2

Mutagenesis

130

1

D → 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

Mutagenesis

130

1

D → E: Weak activity. Ref.2

Mutagenesis

176

1

D → N: Decrease in activity. Ref.2

Mutagenesis

183

1

D → N: No change in activity. Ref.2

Secondary structure

1

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253

Helix Strand Turn

Details...

Beta strand

5 – 13

9

Beta strand

16 – 23

8

Helix

32 – 41

10

Beta strand

46 – 53

8

Beta strand

55 – 57

3

Helix

58 – 70

13

Beta strand

77 – 82

6

Helix

86 – 94

9

Beta strand

98 – 103

6

Helix

104 – 108

5

Helix

111 – 120

10

Helix

122 – 124

3

Beta strand

125 – 134

10

Beta strand

137 – 142

6

Turn

143 – 146

4

Beta strand

147 – 152

6

Helix

153 – 162

10

Beta strand

166 – 172

7

Turn

173 – 177

5

Helix

184 – 190

7

Helix

191 – 193

3

Beta strand

198 – 202

5

Helix

207 – 215

9

Beta strand

219 – 224

6

Helix

225 – 228

4

Beta strand

229 – 232

4

Helix

234 – 243

10

Sequences

	Sequence		Length	Mass (Da)
	Q9X0C6 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: FE0F97F0C57E9025	FASTA	253	27,719
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

C72304.

RefSeq

NP_228842.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	91-253	[»]
3ZR4	X-ray	2.41	A/C/E	1-253	[»]
4EWN	X-ray	1.90	D	1-253	[»]

ProteinModelPortal

Q9X0C6.

SMR

Q9X0C6. Positions 1-251.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59020N.

STRING

243274.TM1036.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAD36113; AAD36113; TM_1036.

GeneID

897046.

KEGG

tma:TM1036.

PATRIC

23937001. VBITheMar51294_1049.

Phylogenomic databases

eggNOG

COG0107.

KO

K02500.

OMA

RVVKGTN.

ProtClustDB

PRK02083.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-467.

UniPathway

UPA00031; UER00010.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_01013. HisF.

InterPro

IPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR004651. HisF.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]

Pfam

PF00977. His_biosynth. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 1 hit.

TIGRFAMs

TIGR00735. hisF. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9X0C6.

Entry information

Entry name

HIS6_THEMA

Accession

Primary (citable) accession number: Q9X0C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2002
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program