ID   HIS7_DESOH              Reviewed;         195 AA.
AC   A8ZUC7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Dole_2155;
OS   Desulfococcus oleovorans (strain DSM 6200 / JCM 39069 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfosudaceae; Desulfosudis.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / JCM 39069 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-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; CP000859; ABW67959.1; -; Genomic_DNA.
DR   RefSeq; WP_012175571.1; NC_009943.1.
DR   AlphaFoldDB; A8ZUC7; -.
DR   SMR; A8ZUC7; -.
DR   STRING; 96561.Dole_2155; -.
DR   EnsemblBacteria; ABW67959; ABW67959; Dole_2155.
DR   KEGG; dol:Dole_2155; -.
DR   eggNOG; COG0131; Bacteria.
DR   HOGENOM; CLU_044308_3_0_7; -.
DR   OMA; ARHGLFD; -.
DR   OrthoDB; 1278103at2; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000008561; 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; 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;
KW   Reference proteome.
FT   CHAIN           1..195
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_1000092689"
SQ   SEQUENCE   195 AA;  21170 MW;  EA1B0CACA664CAD3 CRC64;
     MKRSASVQRQ TAETQVSVTV LLDGIGTQTI STGIPFFNHM LSLFAAHGFF DLTVQASGDI
     DVDFHHTVED VGIVLGNSVN KALGDRKGIR RYGYAVTPMD EALAHAVIDL SNRPFLVFNV
     PSIPAAETGF GVQLAKEFFR AFAVNCGMTL HIRVDYGENE HHVIESVFKA VARALDMATS
     MDDRITGPLS TKGCI