ID   HIS7_STAA2              Reviewed;         192 AA.
AC   A6U561;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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};
GN   OrderedLocusNames=SaurJH1_2757;
OS   Staphylococcus aureus (strain JH1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000736; ABR53579.1; -; Genomic_DNA.
DR   RefSeq; WP_000640266.1; NC_009632.1.
DR   AlphaFoldDB; A6U561; -.
DR   SMR; A6U561; -.
DR   KEGG; sah:SaurJH1_2757; -.
DR   HOGENOM; CLU_044308_3_0_9; -.
DR   OMA; ARHGLFD; -.
DR   UniPathway; UPA00031; UER00011.
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; 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; Cytoplasm; Histidine biosynthesis; Lyase.
FT   CHAIN           1..192
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_1000075256"
SQ   SEQUENCE   192 AA;  21456 MW;  68F9A068091BA280 CRC64;
     MIYQKQRNTA ETQLNISISD DQSPSHINTG VGFLNHMLTL FTFHSGLSLN IEAQGDIDVD
     DHHVTEDIGI VIGQLLLEMI KDKKHFVRYG TMYIPMDETL ARVVVDISGR PYLSFNASLS
     KEKVGTFDTE LVEEFFRAVV INARLTTHID LIRGGNTHHE IEAIFKAFSR ALGIALTATD
     DQRVPSSKGV IE