HIS6_PYRAE
ID HIS6_PYRAE Reviewed; 253 AA.
AC Q8ZY16;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 118.
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=PAE0989;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11679715; DOI=10.1107/s0907444901012604;
RA Banfield M.J., Lott J.S., Arcus V.L., McCarthy A.A., Baker E.N.;
RT "Structure of HisF, a histidine biosynthetic protein from Pyrobaculum
RT aerophilum.";
RL Acta Crystallogr. D 57:1518-1525(2001).
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 -!- 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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; AE009441; AAL63180.1; -; Genomic_DNA.
DR PDB; 1H5Y; X-ray; 2.00 A; A/B=4-253.
DR PDBsum; 1H5Y; -.
DR AlphaFoldDB; Q8ZY16; -.
DR SMR; Q8ZY16; -.
DR STRING; 178306.PAE0989; -.
DR EnsemblBacteria; AAL63180; AAL63180; PAE0989.
DR KEGG; pai:PAE0989; -.
DR PATRIC; fig|178306.9.peg.735; -.
DR eggNOG; arCOG00617; Archaea.
DR HOGENOM; CLU_048577_4_0_2; -.
DR InParanoid; Q8ZY16; -.
DR OMA; IFHYKET; -.
DR BRENDA; 4.3.2.10; 5239.
DR UniPathway; UPA00031; UER00010.
DR EvolutionaryTrace; Q8ZY16; -.
DR Proteomes; UP000002439; 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; Histidine biosynthesis;
KW Lyase; Reference proteome.
FT CHAIN 1..253
FT /note="Imidazole glycerol phosphate synthase subunit HisF"
FT /id="PRO_0000142286"
FT ACT_SITE 12
FT /evidence="ECO:0000255"
FT ACT_SITE 133
FT /evidence="ECO:0000255"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1H5Y"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1H5Y"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1H5Y"
FT TURN 176..181
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1H5Y"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:1H5Y"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1H5Y"
SQ SEQUENCE 253 AA; 26969 MW; 6F91C7A35D04F1A8 CRC64;
MDVALRIIPC LDIDGKAGVV VKGVNFQGIR EVGDPVEMAV RYEEEGADEI AILDITAAPE
GRATFIDSVK RVAEAVSIPV LVGGGVRSLE DATTLFRAGA DKVSVNTAAV RNPQLVALLA
REFGSQSTVV AIDAKWNGEY YEVYVKGGRE ATGLDAVKWA KEVEELGAGE ILLTSIDRDG
TGLGYDVELI RRVADSVRIP VIASGGAGRV EHFYEAAAAG ADAVLAASLF HFRVLSIAQV
KRYLKERGVE VRI
