ID   HIS7_PERMH              Reviewed;         194 AA.
AC   C0QUG8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=PERMA_0544;
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae; Persephonella.
OX   NCBI_TaxID=123214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001230; ACO03794.1; -; Genomic_DNA.
DR   RefSeq; WP_012676033.1; NC_012440.1.
DR   AlphaFoldDB; C0QUG8; -.
DR   SMR; C0QUG8; -.
DR   STRING; 123214.PERMA_0544; -.
DR   EnsemblBacteria; ACO03794; ACO03794; PERMA_0544.
DR   KEGG; pmx:PERMA_0544; -.
DR   eggNOG; COG0131; Bacteria.
DR   HOGENOM; CLU_044308_2_0_0; -.
DR   OMA; ARHGLFD; -.
DR   OrthoDB; 1278103at2; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000001366; 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   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; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR23133; PTHR23133; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Lyase;
KW   Reference proteome.
FT   CHAIN           1..194
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_1000190621"
SQ   SEQUENCE   194 AA;  21481 MW;  DC6BAB94F42B51A1 CRC64;
     MRKASIKRET KETQIELSLN LDGSGKYSID TPVGFLNHML ETFSKHSLID LEVLASGDVH
     VSHHHTVEDV GIVLGMAVKE ALGDKKGIRR FGYAIVPMDE ALSLCSIDIS GRPLLFYDDL
     GLRGKITNFD FELMEEFFKG FTLYSGITVH LKALSGKNLH HIAESLTKSL AVALRQAIEI
     DPRRKDTPST KGSL