HIS7_ASHGO
ID HIS7_ASHGO Reviewed; 220 AA.
AC Q75B47;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE Short=IGPD;
DE EC=4.2.1.19;
GN Name=HIS3; OrderedLocusNames=ADL270C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 6; 12-21 AND 29.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AE016817; AAS51650.2; -; Genomic_DNA.
DR RefSeq; NP_983826.2; NM_209179.2.
DR AlphaFoldDB; Q75B47; -.
DR SMR; Q75B47; -.
DR STRING; 33169.AAS51650; -.
DR EnsemblFungi; AAS51650; AAS51650; AGOS_ADL270C.
DR GeneID; 4619961; -.
DR KEGG; ago:AGOS_ADL270C; -.
DR eggNOG; KOG3143; Eukaryota.
DR HOGENOM; CLU_044308_3_0_1; -.
DR InParanoid; Q75B47; -.
DR OMA; ARHGLFD; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
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; Histidine biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..220
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158233"
SQ SEQUENCE 220 AA; 23675 MW; 6380A800A67169D8 CRC64;
MSETQRAFVK RITHETQVQI ALALNGGPLE IGQSILGGAK TTVAHQASSS QVINVQTGVG
FLDHMIHALA KHSGWSLIVE CVGDLHIDDH HTTEDCGLAL GQALREAIGQ VRGVKRFGTG
FAPLDEALSR AVVDLSNRPY AVVDLGLRRE KIGDLSTEMI PHFLQSFAES ARVTLHVDCL
RGTNDHHRSE SAFKAVAVAL RDALTRTGTD DVPSTKGVLM
