HIS7B_WHEAT
ID HIS7B_WHEAT Reviewed; 269 AA.
AC W5BGD1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase 2, chloroplastic;
DE Short=IGPD 2;
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}.
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DR AlphaFoldDB; W5BGD1; -.
DR SMR; W5BGD1; -.
DR STRING; 4565.Traes_2BL_E1F913FC2.2; -.
DR PRIDE; W5BGD1; -.
DR EnsemblPlants; TraesCS2B02G481000.4; TraesCS2B02G481000.4; TraesCS2B02G481000.
DR Gramene; TraesCS2B02G481000.4; TraesCS2B02G481000.4; TraesCS2B02G481000.
DR HOGENOM; CLU_044308_1_1_1; -.
DR OMA; ARHGLFD; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; W5BGD1; 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 2,
FT chloroplastic"
FT /id="PRO_0000445483"
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; 28720 MW; EF72E5DE0352F620 CRC64;
MTTAPFLFPS LSRLHSARAS SFPKPPVGSG AGVAFPARPY GSSLRLRSSV MAATGVGGNG
SPMAPEESTV SSRLGEVKRV TKETNVHVKI NLDGTGVANS STGIPFLDHM LDQLASHGLF
DVYVKATGDT HIDDHHSNED IALAIGTALL QALGDRKGIN RFGHFTAPLD EAAVEVILDL
SGRPHLSCGL SIPTERVGTY DTQLVEHFFQ SLVNTSGMTL HIRQLAGNNS HHIIEATFKA
FARALRQATE YDLRRQGTIP SSKGVLSRS
