HIS6_THEMA
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 03-AUG-2022, entry version 150.
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; Thermotogae; Thermotogales; Thermotogaceae; 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}.
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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 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 AlphaFoldDB; Q9X0C6; -.
DR BMRB; Q9X0C6; -.
DR SMR; Q9X0C6; -.
DR DIP; DIP-59020N; -.
DR IntAct; Q9X0C6; 1.
DR STRING; 243274.THEMA_09180; -.
DR EnsemblBacteria; AAD36113; AAD36113; TM_1036.
DR KEGG; tma:TM1036; -.
DR eggNOG; COG0107; Bacteria.
DR InParanoid; Q9X0C6; -.
DR OMA; IFHYKET; -.
DR OrthoDB; 1522718at2; -.
DR BioCyc; MetaCyc:MON-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; -; 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 Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00735; hisF; 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 TURN 23..26
FT /evidence="ECO:0007829|PDB:4FX7"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4FX7"
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
