ID   B7A843_THEAQ            Unreviewed;       194 AA.
AC   B7A843;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   10-FEB-2021, entry version 58.
DE   RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_00076, ECO:0000256|RuleBase:RU000599};
DE            Short=IGPD {ECO:0000256|HAMAP-Rule:MF_00076};
DE            EC=4.2.1.19 {ECO:0000256|HAMAP-Rule:MF_00076, ECO:0000256|RuleBase:RU000599};
GN   Name=hisB {ECO:0000256|HAMAP-Rule:MF_00076};
GN   ORFNames=TaqDRAFT_4239 {ECO:0000313|EMBL:EED10430.1};
OS   Thermus aquaticus Y51MC23.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=498848 {ECO:0000313|EMBL:EED10430.1, ECO:0000313|Proteomes:UP000005403};
RN   [1] {ECO:0000313|EMBL:EED10430.1, ECO:0000313|Proteomes:UP000005403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51MC23 {ECO:0000313|EMBL:EED10430.1,
RC   ECO:0000313|Proteomes:UP000005403};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA   Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., Brettin T.S.,
RA   Mead D.;
RT   "Sequencing of the draft genome and assembly of Thermus aquaticus
RT   Y51MC23.";
RL   Submitted (DEC-2008) 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:0000256|HAMAP-Rule:MF_00076,
CC         ECO:0000256|RuleBase:RU000599};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000256|ARBA:ARBA00005047, ECO:0000256|HAMAP-Rule:MF_00076,
CC       ECO:0000256|RuleBase:RU000599}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00076,
CC       ECO:0000256|RuleBase:RU000599}.
CC   -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00076,
CC       ECO:0000256|RuleBase:RU000599}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EED10430.1}.
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DR   EMBL; ABVK02000004; EED10430.1; -; Genomic_DNA.
DR   RefSeq; WP_003046146.1; NZ_CP010822.1.
DR   STRING; 498848.TaqDRAFT_4239; -.
DR   EnsemblBacteria; EED10430; EED10430; TaqDRAFT_4239.
DR   eggNOG; COG0131; Bacteria.
DR   OrthoDB; 1278103at2; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000005403; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00076}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00076};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_00076, ECO:0000256|RuleBase:RU000599};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00076,
KW   ECO:0000256|RuleBase:RU000599, ECO:0000313|EMBL:EED10430.1}.
SQ   SEQUENCE   194 AA;  21345 MW;  9A143C93D92DEE28 CRC64;
     MREALVERAT AETWVRLRLG LDGPVGGKVA TGLPFLDHML LQLQRHGRFL LEVEARGDLE
     VDVHHLVEDV GITLGMALKE ALGEGAGLER YAEAFAPMDE TLVLCVLDLS GRPHLEYRPE
     AWPVVGEAGG VNHYHLREFL RGLVNHGRLT LHLKLLSGRE AHHVLEASFK ALARALHRAT
     RLTGEGLPST KGVL
//