HIS7_CRYNJ
ID HIS7_CRYNJ Reviewed; 202 AA.
AC P0CO22; P40919; Q55J26; Q5KCM8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase;
DE Short=IGPD;
DE EC=4.2.1.19;
GN Name=HIS3; OrderedLocusNames=CNH01620;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-26, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=8045413; DOI=10.1016/0378-1119(94)90336-0;
RA Parker A.R., Moore T.D., Edman J.C., Schwab J.M., Davisson V.J.;
RT "Cloning, sequence analysis and expression of the gene encoding imidazole
RT glycerol phosphate dehydratase in Cryptococcus neoformans.";
RL Gene 145:135-138(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=14724278; DOI=10.1074/jbc.m312733200;
RA Sinha S.C., Chaudhuri B.N., Burgner J.W., Yakovleva G., Davisson V.J.,
RA Smith J.L.;
RT "Crystal structure of imidazole glycerol-phosphate dehydratase: duplication
RT of an unusual fold.";
RL J. Biol. Chem. 279:15491-15498(2004).
CC -!- FUNCTION: Imidazole glycerol-phosphate dehydratase required for
CC histidine biosynthesis. {ECO:0000269|PubMed:8045413}.
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:0000269|PubMed:8045413};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC -!- SUBUNIT: Homotrimer.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000305}.
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DR EMBL; U04329; AAA50951.1; -; Genomic_DNA.
DR EMBL; AE017348; AAW45034.1; -; Genomic_DNA.
DR RefSeq; XP_572341.1; XM_572341.1.
DR PDB; 1RHY; X-ray; 2.30 A; A/B=1-202.
DR PDBsum; 1RHY; -.
DR AlphaFoldDB; P0CO22; -.
DR SMR; P0CO22; -.
DR STRING; 5207.AAW45034; -.
DR PaxDb; P0CO22; -.
DR EnsemblFungi; AAW45034; AAW45034; CNH01620.
DR GeneID; 3259352; -.
DR KEGG; cne:CNH01620; -.
DR VEuPathDB; FungiDB:CNH01620; -.
DR eggNOG; KOG3143; Eukaryota.
DR HOGENOM; CLU_044308_3_0_1; -.
DR InParanoid; P0CO22; -.
DR OMA; ARHGLFD; -.
DR OrthoDB; 1097523at2759; -.
DR BRENDA; 4.2.1.19; 1723.
DR UniPathway; UPA00031; UER00011.
DR EvolutionaryTrace; P0CO22; -.
DR Proteomes; UP000002149; Chromosome 8.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Direct protein sequencing;
KW Histidine biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..202
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /id="PRO_0000158236"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1RHY"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1RHY"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1RHY"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1RHY"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:1RHY"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:1RHY"
FT HELIX 166..185
FT /evidence="ECO:0007829|PDB:1RHY"
SQ SEQUENCE 202 AA; 21976 MW; 619E1E6051C116CC CRC64;
MSERIASVER TTSETHISCT IDLDHIPGVT EQKINVSTGI GFLDHMFTAL AKHGGMSLQL
QCKGDLHIDD HHTAEDCALA LGEAFKKALG ERKGIKRYGY AYAPLDESLS RAVIDISSRP
YFMCHLPFTR EKVGDLSTEM VSHLLQSFAF AAGVTLHIDS IRGENNHHIA ESAFKALALA
IRMAISRTGG DDVPSTKGVL AL
