HIS6_THET8
ID HIS6_THET8 Reviewed; 252 AA.
AC Q7SIB9; Q5SID0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE EC=4.3.2.10 {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase cyclase subunit {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=IGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE AltName: Full=ImGP synthase subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
DE Short=IGPS subunit HisF {ECO:0000255|HAMAP-Rule:MF_01013};
GN Name=hisF {ECO:0000255|HAMAP-Rule:MF_01013}; OrderedLocusNames=TTHA1444;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HISH.
RX PubMed=12417026; DOI=10.1093/oxfordjournals.jbchem.a003284;
RA Omi R., Mizuguchi H., Goto M., Miyahara I., Hayashi H., Kagamiyama H.,
RA Hirotsu K.;
RT "Structure of imidazole glycerol phosphate synthase from Thermus
RT thermophilus HB8: open-closed conformational change and ammonia
RT tunneling.";
RL J. Biochem. 132:759-765(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. {ECO:0000255|HAMAP-Rule:MF_01013}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01013};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
CC {ECO:0000255|HAMAP-Rule:MF_01013}.
CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000255|HAMAP-
CC Rule:MF_01013, ECO:0000269|PubMed:12417026}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01013}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC Rule:MF_01013}.
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DR EMBL; AP008226; BAD71267.1; -; Genomic_DNA.
DR RefSeq; WP_011228686.1; NC_006461.1.
DR RefSeq; YP_144710.1; NC_006461.1.
DR PDB; 1KA9; X-ray; 2.30 A; F=1-252.
DR PDBsum; 1KA9; -.
DR AlphaFoldDB; Q7SIB9; -.
DR SMR; Q7SIB9; -.
DR IntAct; Q7SIB9; 1.
DR STRING; 300852.55772826; -.
DR EnsemblBacteria; BAD71267; BAD71267; BAD71267.
DR GeneID; 3168672; -.
DR KEGG; ttj:TTHA1444; -.
DR PATRIC; fig|300852.9.peg.1418; -.
DR eggNOG; COG0107; Bacteria.
DR HOGENOM; CLU_048577_4_0_0; -.
DR OMA; IFHYKET; -.
DR PhylomeDB; Q7SIB9; -.
DR BRENDA; 4.3.2.10; 2305.
DR UniPathway; UPA00031; UER00010.
DR EvolutionaryTrace; Q7SIB9; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
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; Histidine biosynthesis;
KW Lyase; Reference proteome.
FT CHAIN 1..252
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142255"
FT ACT_SITE 12
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT ACT_SITE 131
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01013"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1KA9"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1KA9"
FT TURN 174..179
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:1KA9"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:1KA9"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:1KA9"
SQ SEQUENCE 252 AA; 26952 MW; 113ED335F307BF43 CRC64;
MSLAKRIVPC LDVHAGRVVK GVNFVNLRDA GDPVEAARAY DEAGADELVF LDISATHEER
AILLDVVARV AERVFIPLTV GGGVRSLEDA RKLLLSGADK VSVNSAAVRR PELIRELADH
FGAQAVVLAI DARWRGDFPE VHVAGGRVPT GLHAVEWAVK GVELGAGEIL LTSMDRDGTK
EGYDLRLTRM VAEAVGVPVI ASGGAGRMEH FLEAFQAGAE AALAASVFHF GEIPIPKLKR
YLAEKGVHVR LD
