ID HIS6_THEMA Reviewed; 253 AA. AC Q9X0C6; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 157. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF; DE EC=4.3.2.10; DE AltName: Full=IGP synthase cyclase subunit; DE AltName: Full=IGP synthase subunit HisF; DE AltName: Full=ImGP synthase subunit HisF; DE Short=IGPS subunit HisF; GN Name=hisF; OrderedLocusNames=TM_1036; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF CYS-9; ASP-11; LYS-19; RP ASP-51; ASN-103; ASP-130; ASP-176 AND ASP-183, BIOPHYSICOCHEMICAL RP PROPERTIES, AND REACTION MECHANISM. RX PubMed=11264293; DOI=10.1074/jbc.m102012200; RA Beismann-Driemeyer S., Sterner R.; RT "Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary RT structure, steady-state kinetics, and reaction mechanism of the bienzyme RT complex."; RL J. Biol. Chem. 276:20387-20396(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX PubMed=10968789; DOI=10.1126/science.289.5484.1546; RA Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.; RT "Structural evidence for evolution of the beta/alpha barrel scaffold by RT gene duplication and fusion."; RL Science 289:1546-1550(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=11839304; DOI=10.1016/s0969-2126(02)00702-5; RA Douangamath A., Walker M., Beismann-Driemeyer S., Vega-Fernandez M.C., RA Sterner R., Wilmanns M.; RT "Structural evidence for ammonia tunneling across the (beta alpha)(8) RT barrel of the imidazole glycerol phosphate synthase bienzyme complex."; RL Structure 10:185-193(2002). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, CC AICAR and glutamate. The HisF subunit catalyzes the cyclization CC activity that produces IGP and AICAR from PRFAR using the ammonia CC provided by the HisH subunit. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5- CC amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D- CC erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate; CC Xref=Rhea:RHEA:24793, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58278, ChEBI:CHEBI:58359, ChEBI:CHEBI:58475, CC ChEBI:CHEBI:58525; EC=4.3.2.10; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.5 uM for PRFAR {ECO:0000269|PubMed:11264293}; CC KM=2.2 mM for NH(3) {ECO:0000269|PubMed:11264293}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. CC -!- INTERACTION: CC Q9X0C6; Q9X0C8: hisH; NbExp=2; IntAct=EBI-9026911, EBI-9026913; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000512; AAD36113.1; -; Genomic_DNA. DR PIR; C72304; C72304. DR RefSeq; NP_228842.1; NC_000853.1. DR RefSeq; WP_004080486.1; NZ_CP011107.1. DR PDB; 1GPW; X-ray; 2.40 A; A/C/E=1-253. DR PDB; 1THF; X-ray; 1.45 A; D=1-253. DR PDB; 1VH7; X-ray; 1.90 A; A=2-253. DR PDB; 2A0N; X-ray; 1.64 A; A=1-253. DR PDB; 2LLE; NMR; -; A=103-247. DR PDB; 2W6R; X-ray; 2.10 A; A=123-253. DR PDB; 2WJZ; X-ray; 2.60 A; A/C/E=1-253. DR PDB; 3CWO; X-ray; 3.10 A; X=103-253. DR PDB; 3OG3; X-ray; 2.08 A; A=43-221. DR PDB; 3ZR4; X-ray; 2.41 A; A/C/E=1-253. DR PDB; 4EWN; X-ray; 1.90 A; D=1-253. DR PDB; 4FX7; X-ray; 2.08 A; A/B/C/D=99-219. DR PDB; 4J9J; X-ray; 2.30 A; A=91-220. DR PDB; 5TQL; X-ray; 1.90 A; A/B=2-253. DR PDB; 6RTZ; X-ray; 2.87 A; A=1-253. DR PDB; 6RU0; X-ray; 2.65 A; A/C/E=1-253. DR PDB; 6VDG; X-ray; 2.79 A; A=1-253. DR PDB; 6YMU; X-ray; 2.11 A; A/C/E=1-253. DR PDB; 7AC8; X-ray; 2.06 A; A/C/E=1-253. DR PDB; 7QC3; X-ray; 1.65 A; A=2-253. DR PDB; 7QC6; X-ray; 2.10 A; A=2-253. DR PDB; 7QC7; X-ray; 1.60 A; A=2-253. DR PDB; 7QC8; X-ray; 1.80 A; A=2-253. DR PDB; 7QC9; X-ray; 1.80 A; A=2-253. DR PDBsum; 1GPW; -. DR PDBsum; 1THF; -. DR PDBsum; 1VH7; -. DR PDBsum; 2A0N; -. DR PDBsum; 2LLE; -. DR PDBsum; 2W6R; -. DR PDBsum; 2WJZ; -. DR PDBsum; 3CWO; -. DR PDBsum; 3OG3; -. DR PDBsum; 3ZR4; -. DR PDBsum; 4EWN; -. DR PDBsum; 4FX7; -. DR PDBsum; 4J9J; -. DR PDBsum; 5TQL; -. DR PDBsum; 6RTZ; -. DR PDBsum; 6RU0; -. DR PDBsum; 6VDG; -. DR PDBsum; 6YMU; -. DR PDBsum; 7AC8; -. DR PDBsum; 7QC3; -. DR PDBsum; 7QC6; -. DR PDBsum; 7QC7; -. DR PDBsum; 7QC8; -. DR PDBsum; 7QC9; -. DR AlphaFoldDB; Q9X0C6; -. DR BMRB; Q9X0C6; -. DR SMR; Q9X0C6; -. DR DIP; DIP-59020N; -. DR IntAct; Q9X0C6; 1. DR STRING; 243274.TM_1036; -. DR PaxDb; 243274-THEMA_09180; -. DR EnsemblBacteria; AAD36113; AAD36113; TM_1036. DR KEGG; tma:TM1036; -. DR eggNOG; COG0107; Bacteria. DR InParanoid; Q9X0C6; -. DR OrthoDB; 9781903at2; -. DR BioCyc; MetaCyc:MONOMER-467; -. DR BRENDA; 4.3.1.B2; 6331. DR BRENDA; 4.3.2.10; 6331. DR SABIO-RK; Q9X0C6; -. DR UniPathway; UPA00031; UER00010. DR EvolutionaryTrace; Q9X0C6; -. DR PRO; PR:Q9X0C6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd04731; HisF; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01013; HisF; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR004651; HisF. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR00735; hisF; 1. DR PANTHER; PTHR21235:SF2; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF; 1. DR PANTHER; PTHR21235; IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE SUBUNIT HISF/H IGP SYNTHASE SUBUNIT HISF/H; 1. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; KW Direct protein sequencing; Histidine biosynthesis; Lyase; KW Reference proteome. FT CHAIN 1..253 FT /note="Imidazole glycerol phosphate synthase subunit HisF" FT /id="PRO_0000142253" FT ACT_SITE 11 FT /evidence="ECO:0000255" FT ACT_SITE 130 FT /evidence="ECO:0000255" FT MUTAGEN 9 FT /note="C->A: No change in activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 11 FT /note="D->X: Loss of activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 19 FT /note="K->S: Decrease in activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 51 FT /note="D->N: No change in activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 103 FT /note="N->A: No change in activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 130 FT /note="D->A,C,F,G,H,I,K,L,M,N,P,Q,R,S,T,V,W,Y: Complete FT loss of activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 130 FT /note="D->E: Weak activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 176 FT /note="D->N: Decrease in activity." FT /evidence="ECO:0000269|PubMed:11264293" FT MUTAGEN 183 FT /note="D->N: No change in activity." FT /evidence="ECO:0000269|PubMed:11264293" FT STRAND 5..13 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 16..21 FT /evidence="ECO:0007829|PDB:4FX7" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:7QC3" FT HELIX 32..41 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 58..70 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 86..94 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 104..108 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 111..120 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 125..134 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 137..142 FT /evidence="ECO:0007829|PDB:1THF" FT TURN 143..146 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 153..162 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 166..172 FT /evidence="ECO:0007829|PDB:1THF" FT TURN 173..177 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 184..190 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:1THF" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:1GPW" FT HELIX 234..243 FT /evidence="ECO:0007829|PDB:1THF" FT STRAND 250..253 FT /evidence="ECO:0007829|PDB:3CWO" SQ SEQUENCE 253 AA; 27719 MW; FE0F97F0C57E9025 CRC64; MLAKRIIACL DVKDGRVVKG TNFENLRDSG DPVELGKFYS EIGIDELVFL DITASVEKRK TMLELVEKVA EQIDIPFTVG GGIHDFETAS ELILRGADKV SINTAAVENP SLITQIAQTF GSQAVVVAID AKRVDGEFMV FTYSGKKNTG ILLRDWVVEV EKRGAGEILL TSIDRDGTKS GYDTEMIRFV RPLTTLPIIA SGGAGKMEHF LEAFLAGADA ALAASVFHFR EIDVRELKEY LKKHGVNVRL EGL //