HIS7_PEA
ID HIS7_PEA Reviewed; 281 AA.
AC Q43072;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase, chloroplastic {ECO:0000303|Ref.1};
DE Short=IGPD {ECO:0000303|Ref.1};
DE EC=4.2.1.19 {ECO:0000250|UniProtKB:O23346};
DE Flags: Precursor;
GN Name=HIS3 {ECO:0000303|Ref.1};
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Alaska;
RA Kim J., Theologis A.;
RT "Cloning a cDNA encoding imidazoleglycerol-phosphate dehydratase, the Yeast
RT HIS3 homolog from pea.";
RL (er) Plant Gene Register PGR96-033(1996).
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:0000250|UniProtKB:O23346};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O23346};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000250|UniProtKB:O23346};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC {ECO:0000250|UniProtKB:O23346}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase
CC family. {ECO:0000305}.
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DR EMBL; U49978; AAB67738.1; -; mRNA.
DR PIR; T06530; T06530.
DR AlphaFoldDB; Q43072; -.
DR SMR; Q43072; -.
DR UniPathway; UPA00031; UER00011.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Chloroplast; Histidine biosynthesis; Lyase;
KW Manganese; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..85
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 86..281
FT /note="Imidazoleglycerol-phosphate dehydratase,
FT chloroplastic"
FT /id="PRO_0000158255"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 121..129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 147..151
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 148
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 243..251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 273..275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
SQ SEQUENCE 281 AA; 30766 MW; 402F8E6AEEE112A3 CRC64;
MELYAASHSL PNYPSSFLFK PKITTFHTTL FPTKFAPFKA SFFSPNHLTL TTPMNPPTTS
LSSAAFVEHN NGSTSTSLPF HPETRVGEVK RVTKETNVSV KINLDGSGVA DSSTGIPFLD
HMLDQLASHG LFDVHVKATG DVHIDDHHTN EDVALAIGTA LLQALGDRKG INRFGDFSAP
LDEALIHVSL DLSGRPHLSY NLDIPTQRVG TYDTQVVEHF LQSIVNTSGM TLHIRQLAGR
NSHHIIEATF KAFARALRQA TEYDPRRRGS VPSSKGVLSR S
