ID B7A843_THEAQ Unreviewed; 194 AA. AC B7A843; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 20-JAN-2016, entry version 32. DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_00076, ECO:0000256|RuleBase:RU000599, ECO:0000256|SAAS:SAAS00348983}; 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, ECO:0000256|SAAS:SAAS00406463}; GN Name=hisB {ECO:0000256|HAMAP-Rule:MF_00076}; GN ORFNames=TaqDRAFT_4239 {ECO:0000313|EMBL:EED10430.1}, TO73_1557 GN {ECO:0000313|EMBL:ALJ91398.1}; 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. RN [2] {ECO:0000313|EMBL:ALJ91398.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Y51MC23 {ECO:0000313|EMBL:ALJ91398.1}; RA Brumm P., Monsma S., Mead D.A., Keough B., Jasinovica S., Ferguson E., RA Schoenfeld T., Lodes M.; RT "Complete Genome Sequence of Thermus aquaticus Y51MC23."; RL Submitted (APR-2015) 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|HAMAP-Rule:MF_00076, ECO:0000256|RuleBase:RU000599, CC ECO:0000256|SAAS:SAAS00406440}. 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|HAMAP-Rule:MF_00076, ECO:0000256|RuleBase:RU000599, CC ECO:0000256|SAAS:SAAS00406454}. 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 --------------------------------------------------------------------------- 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; CP010822; ALJ91398.1; -; Genomic_DNA. DR EMBL; ABVK02000004; EED10430.1; -; Genomic_DNA. DR RefSeq; WP_003046146.1; NZ_ABVK02000004.1. DR STRING; 498848.TaqDRAFT_4239; -. DR EnsemblBacteria; EED10430; EED10430; TaqDRAFT_4239. DR PATRIC; 25941347; VBITheAqu66851_1077. DR eggNOG; COG0131; LUCA. DR eggNOG; ENOG4105ECC; Bacteria. 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|HAMAP-Rule:MF_00076, KW ECO:0000256|SAAS:SAAS00131101}; KW Complete proteome {ECO:0000313|Proteomes:UP000005403}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00076}; KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00076, KW ECO:0000256|RuleBase:RU000599, ECO:0000256|SAAS:SAAS00131080}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00076, ECO:0000256|RuleBase:RU000599, KW ECO:0000256|SAAS:SAAS00131081, 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 //