ID   HIS7_CHLPM              Reviewed;         200 AA.
AC   A4SF66;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Cvib_1111;
OS   Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris
OS   vibrioformis (strain DSM 265)).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=290318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 265 / 1930;
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., Pitluck S., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J.,
RA   Schuster S.C., Bryant D.A., Richardson P.;
RT   "Complete sequence of Prosthecochloris vibrioformis DSM 265.";
RL   Submitted (MAR-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; CP000607; ABP37125.1; -; Genomic_DNA.
DR   RefSeq; WP_011890348.1; NC_009337.1.
DR   AlphaFoldDB; A4SF66; -.
DR   SMR; A4SF66; -.
DR   STRING; 290318.Cvib_1111; -.
DR   EnsemblBacteria; ABP37125; ABP37125; Cvib_1111.
DR   KEGG; pvi:Cvib_1111; -.
DR   eggNOG; COG0131; Bacteria.
DR   HOGENOM; CLU_044308_3_0_10; -.
DR   OMA; ARHGLFD; -.
DR   OrthoDB; 1278103at2; -.
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..200
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_0000336334"
SQ   SEQUENCE   200 AA;  21741 MW;  38118790572E0DDA CRC64;
     MAEQEEKQTR RATAARKTQE TDITISISLD GTGSSSIESG IGFLDHMLTS FSRHSGIDIT
     LQCQGDLVVD DHHTVEDIAI VLGGAITEAL GEKRGIRRYG WAMIPMDEAL ARCAVDLGGR
     SCSVFRAEFS RPLIEGLSTE MVEHFFTSLA GSMNANIHIA ILEGRNTHHK IEAIFKAFAY
     AMKDAIKVEG NAVPSTKGVF