HIS7A_WHEAT
ID HIS7A_WHEAT Reviewed; 269 AA.
AC P34048; A0A1D5UIZ1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Imidazoleglycerol-phosphate dehydratase 1, chloroplastic;
DE Short=IGPD 1;
DE EC=4.2.1.19 {ECO:0000250|UniProtKB:O23346};
DE Flags: Precursor;
GN ORFNames=CAMPLR22A2D_LOCUS4590 {ECO:0000312|EMBL:SPT19963.1};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-269.
RA Tada S., Volrath S., Guyer D., Scheidegger A., Ryals J., Ohta D., Ward E.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA93197.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; LS480641; SPT19963.1; -; Genomic_DNA.
DR EMBL; U02690; AAA93197.1; ALT_INIT; mRNA.
DR PIR; T06261; T06261.
DR AlphaFoldDB; P34048; -.
DR SMR; P34048; -.
DR PRIDE; P34048; -.
DR EnsemblPlants; TraesCS2D02G459900.3; TraesCS2D02G459900.3; TraesCS2D02G459900.
DR Gramene; TraesCS2D02G459900.3; TraesCS2D02G459900.3; TraesCS2D02G459900.
DR eggNOG; KOG3143; Eukaryota.
DR OMA; STHTCDS; -.
DR UniPathway; UPA00031; UER00011.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P34048; 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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Chloroplast; Histidine biosynthesis; Lyase;
KW Manganese; Metal-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..269
FT /note="Imidazoleglycerol-phosphate dehydratase 1,
FT chloroplastic"
FT /id="PRO_0000158256"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 259
FT /note="I -> M (in Ref. 2; AAA93197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28632 MW; 80AFE1C4A87AAB86 CRC64;
MTTAPFVSPS LPRLHSARAS PFPKPSVGSG GGVAFPARTY GSSLRLRSAV MSASGVGGNG
SPMAPEESTV SSRLGEVKRV TKETNVHVKI NLDGTGVANS STGIPFLDHM LDQLASHGLF
DVYVKATGDT HIDDHHSNED IALAIGTALL QALGDRKGIN RFGHFTAPLD EAAVEVILDL
SGRPHLSCGL SIPTERVGTY DTQLVEHFFQ SLVNTSGMTL HIRQLAGNNS HHIIEATFKA
FARALRQATE YDLRRQGTIP SSKGVLSRS
