ID B7A843_THEAQ Unreviewed; 194 AA. AC B7A843; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 11-MAY-2016, entry version 35. DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|SAAS:SAAS00218099}; DE EC=4.2.1.19 {ECO:0000256|SAAS:SAAS00263879}; GN ORFNames=TaqDRAFT_4239 {ECO:0000313|EMBL:EED10430.1}; OS Thermus aquaticus Y51MC23. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC 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., RA Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., RA Hauser L., Saunders E., Tapia R., Green L., Rogers Y., Detter J.C., RA Brettin T.S., 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: D-erythro-1-(imidazol-4-yl)glycerol 3- CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. CC {ECO:0000256|SAAS:SAAS00131085}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. CC {ECO:0000256|SAAS:SAAS00131107}. CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase CC family. {ECO:0000256|SAAS:SAAS00590873}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EED10430.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; taq:TO73_1557; -. DR PATRIC; 25941347; VBITheAqu66851_1077. DR eggNOG; ENOG4105ECC; Bacteria. DR eggNOG; COG0131; LUCA. DR KO; K01693; -. 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-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00076; HisB; 1. DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase. DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR PANTHER; PTHR23133:SF2; PTHR23133:SF2; 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|SAAS:SAAS00484728}; KW Complete proteome {ECO:0000313|Proteomes:UP000005403}; KW Histidine biosynthesis {ECO:0000256|SAAS:SAAS00484639}; KW Lyase {ECO:0000256|SAAS:SAAS00484556, 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 //