HIS7_PYRFU
ID HIS7_PYRFU Reviewed; 176 AA.
AC P58880;
DT 24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_00076};
DE Short=IGPD {ECO:0000255|HAMAP-Rule:MF_00076};
DE EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_00076};
GN Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076}; OrderedLocusNames=PF1660;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC 4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00076};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC {ECO:0000255|HAMAP-Rule:MF_00076}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00076}.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000255|HAMAP-Rule:MF_00076}.
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DR EMBL; AE009950; AAL81784.1; -; Genomic_DNA.
DR RefSeq; WP_011012806.1; NZ_CP023154.1.
DR PDB; 5DNL; X-ray; 1.53 A; A/B/C=1-176.
DR PDB; 5DNX; X-ray; 1.80 A; A/B/C=1-176.
DR PDBsum; 5DNL; -.
DR PDBsum; 5DNX; -.
DR AlphaFoldDB; P58880; -.
DR SMR; P58880; -.
DR STRING; 186497.PF1660; -.
DR EnsemblBacteria; AAL81784; AAL81784; PF1660.
DR GeneID; 41713488; -.
DR KEGG; pfu:PF1660; -.
DR PATRIC; fig|186497.12.peg.1726; -.
DR eggNOG; arCOG04398; Archaea.
DR HOGENOM; CLU_044308_2_1_2; -.
DR OMA; ARHGLFD; -.
DR OrthoDB; 91418at2157; -.
DR PhylomeDB; P58880; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.40; -; 2.
DR HAMAP; MF_00076; HisB; 1.
DR InterPro; IPR038494; IGPD_sf.
DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR23133; PTHR23133; 1.
DR Pfam; PF00475; IGPD; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Lyase; Reference proteome.
FT CHAIN 1..176
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158195"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:5DNL"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:5DNL"
FT HELIX 51..69
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5DNL"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:5DNL"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:5DNL"
FT HELIX 144..162
FT /evidence="ECO:0007829|PDB:5DNL"
SQ SEQUENCE 176 AA; 19736 MW; DF449AA227D09133 CRC64;
MRRTTKETDI IVEIGKKGEI KTNDLILDHM LTAFAFYLGK DMRITATYDL RHHLWEDIGI
TLGEALRENL PEKFTRFGNA IMPMDDALVL VSVDISNRPY ANVDVNIKDA EEGFAVSLLK
EFVWGLARGL RATIHIKQLS GENAHHIVEA AFKGLGMALR VATKESERVE STKGVL
