HIS7_YEAST
ID HIS7_YEAST Reviewed; 220 AA.
AC P06633; D6W2Q9; Q12695; Q70D78; Q70D79; Q70D81; Q70D83;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE Short=IGPD;
DE EC=4.2.1.19 {ECO:0000250|UniProtKB:P9WML9};
GN Name=HIS3 {ECO:0000303|PubMed:3001645}; OrderedLocusNames=YOR202W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3001645; DOI=10.1093/nar/13.23.8587;
RA Struhl K.;
RT "Nucleotide sequence and transcriptional mapping of the yeast pet56-his3-
RT ded1 gene region.";
RL Nucleic Acids Res. 13:8587-8601(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtz A., Lou Y.;
RT "pHISi-1, complete sequence.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-8; LEU-30; ALA-92 AND
RP ASN-216.
RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=6173490; DOI=10.1016/0022-2836(81)90268-0;
RA Struhl K., Davis R.W.;
RT "Promotor mutants of the yeast his3 gene.";
RL J. Mol. Biol. 152:553-568(1981).
RN [7]
RP INDUCTION.
RX PubMed=3532321; DOI=10.1126/science.3532321;
RA Hill D.E., Hope I.A., Macke J.P., Struhl K.;
RT "Saturation mutagenesis of the yeast his3 regulatory site: requirements for
RT transcriptional induction and for binding by GCN4 activator protein.";
RL Science 234:451-457(1986).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) IN COMPLEX WITH MANGANESE
RP AND C348.
RX PubMed=29434040; DOI=10.1073/pnas.1708839115;
RA Rawson S., Bisson C., Hurdiss D.L., Fazal A., McPhillie M.J.,
RA Sedelnikova S.E., Baker P.J., Rice D.W., Muench S.P.;
RT "Elucidating the structural basis for differing enzyme inhibitor potency by
RT cryo-EM.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1795-1800(2018).
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:0000250|UniProtKB:P9WML9};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:29434040};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:29434040};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC {ECO:0000250|UniProtKB:P9WML9}.
CC -!- INDUCTION: Induced by histidine starvation in a GCN4-dependent manner.
CC {ECO:0000269|PubMed:3532321}.
CC -!- MISCELLANEOUS: Present with 2100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000305}.
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DR EMBL; X03245; CAA27003.1; -; Genomic_DNA.
DR EMBL; U89927; AAB64382.1; -; Genomic_DNA.
DR EMBL; U89928; AAB64385.1; -; Genomic_DNA.
DR EMBL; AJ585705; CAE52225.1; -; Genomic_DNA.
DR EMBL; AJ585706; CAE52226.1; -; Genomic_DNA.
DR EMBL; AJ585707; CAE52227.1; -; Genomic_DNA.
DR EMBL; AJ585708; CAE52228.1; -; Genomic_DNA.
DR EMBL; AJ585709; CAE52229.1; -; Genomic_DNA.
DR EMBL; AJ585710; CAE52230.1; -; Genomic_DNA.
DR EMBL; AJ585711; CAE52231.1; -; Genomic_DNA.
DR EMBL; AJ585712; CAE52232.1; -; Genomic_DNA.
DR EMBL; AJ585713; CAE52233.1; -; Genomic_DNA.
DR EMBL; AJ585714; CAE52234.1; -; Genomic_DNA.
DR EMBL; AJ585715; CAE52235.1; -; Genomic_DNA.
DR EMBL; AJ585716; CAE52236.1; -; Genomic_DNA.
DR EMBL; AJ585717; CAE52237.1; -; Genomic_DNA.
DR EMBL; AJ585718; CAE52238.1; -; Genomic_DNA.
DR EMBL; AJ585719; CAE52239.1; -; Genomic_DNA.
DR EMBL; Z75110; CAA99417.1; -; Genomic_DNA.
DR EMBL; J01330; AAA88723.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10975.1; -; Genomic_DNA.
DR PIR; S67094; DWBYH.
DR RefSeq; NP_014845.1; NM_001183621.1.
DR PDB; 6EZM; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-220.
DR PDBsum; 6EZM; -.
DR AlphaFoldDB; P06633; -.
DR SMR; P06633; -.
DR BioGRID; 34598; 53.
DR DIP; DIP-6759N; -.
DR IntAct; P06633; 8.
DR MINT; P06633; -.
DR STRING; 4932.YOR202W; -.
DR PaxDb; P06633; -.
DR PRIDE; P06633; -.
DR EnsemblFungi; YOR202W_mRNA; YOR202W; YOR202W.
DR GeneID; 854377; -.
DR KEGG; sce:YOR202W; -.
DR SGD; S000005728; HIS3.
DR VEuPathDB; FungiDB:YOR202W; -.
DR eggNOG; KOG3143; Eukaryota.
DR HOGENOM; CLU_044308_3_0_1; -.
DR InParanoid; P06633; -.
DR OMA; ARHGLFD; -.
DR BioCyc; YEAST:YOR202W-MON; -.
DR UniPathway; UPA00031; UER00011.
DR PRO; PR:P06633; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P06633; protein.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IDA:SGD.
DR CDD; cd07914; IGPD; 1.
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; PS00954; IGP_DEHYDRATASE_1; 1.
DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Histidine biosynthesis; Lyase;
KW Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..220
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158250"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 64..72
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 90..94
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 94
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 186..194
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 190
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:29434040,
FT ECO:0007744|PDB:6EZM"
FT VARIANT 8
FT /note="V -> I (in strain: CLIB 219)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 30
FT /note="I -> L (in strain: CLIB 219, CLIB 410, CLIB 413 and
FT YIIc17 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 92
FT /note="T -> A (in strain: YIIc12 and YIIc17 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 216
FT /note="K -> N (in strain: YIIc17 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT CONFLICT 109..111
FT /note="GAV -> LA (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:6EZM"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:6EZM"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6EZM"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6EZM"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6EZM"
FT HELIX 185..203
FT /evidence="ECO:0007829|PDB:6EZM"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6EZM"
SQ SEQUENCE 220 AA; 23833 MW; C50AC3B3554A9554 CRC64;
MTEQKALVKR ITNETKIQIA ISLKGGPLAI EHSIFPEKEA EAVAEQATQS QVINVHTGIG
FLDHMIHALA KHSGWSLIVE CIGDLHIDDH HTTEDCGIAL GQAFKEALGA VRGVKRFGSG
FAPLDEALSR AVVDLSNRPY AVVELGLQRE KVGDLSCEMI PHFLESFAEA SRITLHVDCL
RGKNDHHRSE SAFKALAVAI REATSPNGTN DVPSTKGVLM
