HIS7C_WHEAT
ID HIS7C_WHEAT Reviewed; 269 AA.
AC W5AWH5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase 3, chloroplastic;
DE Short=IGPD 3;
DE EC=4.2.1.19 {ECO:0000250|UniProtKB:O23346};
DE Flags: Precursor;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=23192148; DOI=10.1038/nature11650;
RA Brenchley R., Spannagl M., Pfeifer M., Barker G.L., D'Amore R., Allen A.M.,
RA McKenzie N., Kramer M., Kerhornou A., Bolser D., Kay S., Waite D.,
RA Trick M., Bancroft I., Gu Y., Huo N., Luo M.C., Sehgal S., Gill B.,
RA Kianian S., Anderson O., Kersey P., Dvorak J., McCombie W.R., Hall A.,
RA Mayer K.F., Edwards K.J., Bevan M.W., Hall N.;
RT "Analysis of the bread wheat genome using whole-genome shotgun
RT sequencing.";
RL Nature 491:705-710(2012).
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}.
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 AlphaFoldDB; W5AWH5; -.
DR SMR; W5AWH5; -.
DR STRING; 4565.Traes_2AL_BF1F0B29A.2; -.
DR EnsemblPlants; TraesCS2A02G459600.1; TraesCS2A02G459600.1; TraesCS2A02G459600.
DR EnsemblPlants; TraesPAR_scaffold_124777_01G000100.1; TraesPAR_scaffold_124777_01G000100.1; TraesPAR_scaffold_124777_01G000100.
DR EnsemblPlants; TraesROB_scaffold_054236_01G000100.1; TraesROB_scaffold_054236_01G000100.1; TraesROB_scaffold_054236_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_025508_01G000300.1; TraesWEE_scaffold_025508_01G000300.1; TraesWEE_scaffold_025508_01G000300.
DR Gramene; TraesCS2A02G459600.1; TraesCS2A02G459600.1; TraesCS2A02G459600.
DR Gramene; TraesPAR_scaffold_124777_01G000100.1; TraesPAR_scaffold_124777_01G000100.1; TraesPAR_scaffold_124777_01G000100.
DR Gramene; TraesROB_scaffold_054236_01G000100.1; TraesROB_scaffold_054236_01G000100.1; TraesROB_scaffold_054236_01G000100.
DR Gramene; TraesWEE_scaffold_025508_01G000300.1; TraesWEE_scaffold_025508_01G000300.1; TraesWEE_scaffold_025508_01G000300.
DR eggNOG; KOG3143; Eukaryota.
DR HOGENOM; CLU_044308_1_1_1; -.
DR OMA; HTEPENI; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; W5AWH5; baseline.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Chloroplast; Histidine biosynthesis; Lyase;
KW Manganese; Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 52..269
FT /note="Imidazoleglycerol-phosphate dehydratase 3,
FT chloroplastic"
FT /id="PRO_0000445484"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 109..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 109
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 135..139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 207
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 231..239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 231
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O23346"
FT BINDING 261..263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O23346"
SQ SEQUENCE 269 AA; 28501 MW; BC1B1EF48F1A6DED CRC64;
MTTAPVVSPS LSRLHSAPAS PFPKAPVGSG AGVAFPARPY GPSLRLRSAV MAASGVGGNG
SPMAPEESAV SSRLGEVKRV TKETNVHVKI NLDGTGVANS STGIPFLDHM LDQLASHGLF
DVYVKATGDT HIDDHHSNED IALAIGTALL QALGDRKGIN RFGHFTAPLD EAAVEVILDL
SGRPHLSCGL SIPTERVGTY DTQLVEHFFQ SLVNTSGMTL HIRQLAGNNS HHIIEATFKA
FARALRQATE YDLRRRGTIP SSKGVLSRS
