HIS7_DESHY
ID HIS7_DESHY Reviewed; 196 AA.
AC Q24QJ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=DSY3911;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51;
RX PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85700.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24QJ2; -.
DR SMR; Q24QJ2; -.
DR STRING; 138119.DSY3911; -.
DR EnsemblBacteria; BAE85700; BAE85700; DSY3911.
DR KEGG; dsy:DSY3911; -.
DR eggNOG; COG0131; Bacteria.
DR HOGENOM; CLU_044308_3_0_9; -.
DR OMA; ARHGLFD; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000001946; 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..196
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000336310"
SQ SEQUENCE 196 AA; 21808 MW; 90026E990E415C7B CRC64;
MEMREAYIER QTKETRIRVK LNLDGAGTAQ VDTGIGFFDH MLEALARFGY LDLEVAAEGD
LQVDPHHTIE DCGLVFGQAI REALGERRGI ERVGDTLLPM DEALVQVALD LSNRPYLVWD
VECPEGMVGG FPVEMAEEFF RAVSVQAGIT LHIRLFSGKN RHHILEAIFK GFGRALGLAL
RENPRFQGVL STKGVL