ID   HIS7_PICST              Reviewed;         222 AA.
AC   Q9C1D4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE            Short=IGPD;
DE            EC=4.2.1.19;
GN   Name=HIS3;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 62970 / CBS 5774 / NRRL Y-11542;
RA   Schruff B.S., Klinner U.;
RT   "Pichia stipitis HIS3 gene.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC   -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; AF348970; AAK27156.1; -; Genomic_DNA.
DR   EMBL; CP000498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q9C1D4; -.
DR   SMR; Q9C1D4; -.
DR   STRING; 322104.Q9C1D4; -.
DR   InParanoid; Q9C1D4; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Histidine biosynthesis; Lyase; Reference proteome.
FT   CHAIN           1..222
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_0000158245"
FT   CONFLICT        177
FT                   /note="M -> T (in Ref. 1; AAK27156)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24087 MW;  D99298A3777E0017 CRC64;
     MARTATIKRD TNETKIQIAL SLDGGFLAVE ESIFKKRKID DDDEHAKQAT SSQVINVQSG
     IGFLDHMLHA LAKHAGWSLI VECIGDLHID DHHTAEDVGI TLGIAFKQAL GQVKGVKRFG
     SGFAPLDEAL SRAVVDLSNR PFAVVELGLK REKIGDLSCE MIPHVLESFA QGAHITMHVD
     CLRGFNDHHR AESAFKALAV AIREAISSNG TNDVPSTKGV LF