ID   HIS7_CORGL              Reviewed;         202 AA.
AC   Q9KJU3;
DT   24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=Cgl2100, cg2303;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA   Han M.S., Jung S.I., Chun J.Y., Lee M.-S.;
RT   "Molecular cloning of hisB gene from Corynebacterium glutamicum.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; AF160479; AAF80391.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB99493.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20436.1; -; Genomic_DNA.
DR   RefSeq; NP_601299.1; NC_003450.3.
DR   RefSeq; WP_003861983.1; NC_006958.1.
DR   AlphaFoldDB; Q9KJU3; -.
DR   SMR; Q9KJU3; -.
DR   STRING; 196627.cg2303; -.
DR   KEGG; cgb:cg2303; -.
DR   KEGG; cgl:Cgl2100; -.
DR   PATRIC; fig|196627.13.peg.2037; -.
DR   eggNOG; COG0131; Bacteria.
DR   HOGENOM; CLU_044308_2_0_11; -.
DR   OMA; ARHGLFD; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000000582; 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..202
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /id="PRO_0000158127"
FT   CONFLICT        3
FT                   /note="V -> L (in Ref. 1; AAF80391)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38..42
FT                   /note="PFFDH -> HFSTN (in Ref. 1; AAF80391)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62..67
FT                   /note="DIEIDA -> QTSRST (in Ref. 1; AAF80391)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80..87
FT                   /note="QALLDAIG -> KHSLRYC (in Ref. 1; AAF80391)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="G -> D (in Ref. 1; AAF80391)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191..202
FT                   /note="RQTGIPSTKGAL -> IPSLRERFTHELFYHL (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   202 AA;  21914 MW;  3CACB108F7305019 CRC64;
     MTVAPRIGTA TRTTSESDIT VEINLDGTGK VDIDTGLPFF DHMLTAFGVH GSFDLKVHAK
     GDIEIDAHHT VEDTAIVLGQ ALLDAIGDKK GIRRFASCQL PMDEALVESV VDISGRPYFV
     ISGEPDHMIT SVIGGHYATV INEHFFETLA LNSRITLHVI CHYGRDPHHI TEAEYKAVAR
     ALRGAVEMDP RQTGIPSTKG AL