ID   HIS8_NICPL              Reviewed;         413 AA.
AC   Q9FEW2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Histidinol-phosphate aminotransferase, chloroplastic;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
DE   Flags: Precursor;
GN   Name=HPA;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTANT HIS1-.
RC   TISSUE=Leaf;
RX   PubMed=11289510; DOI=10.1023/a:1006493021557;
RA   El Malki F., Jacobs M.;
RT   "Molecular characterization and expression study of a histidine auxotrophic
RT   mutant (his1-) of Nicotiana plumbaginifolia.";
RL   Plant Mol. Biol. 45:191-199(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC         oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:57980; EC=2.6.1.9;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in flowers, leaves, stems and roots.
CC       {ECO:0000269|PubMed:11289510}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {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   EMBL; AJ278767; CAC20728.1; -; mRNA.
DR   AlphaFoldDB; Q9FEW2; -.
DR   SMR; Q9FEW2; -.
DR   UniPathway; UPA00031; UER00012.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aminotransferase; Chloroplast;
KW   Histidine biosynthesis; Plastid; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..413
FT                   /note="Histidinol-phosphate aminotransferase,
FT                   chloroplastic"
FT                   /id="PRO_0000013448"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         381
FT                   /note="R->H: In His1-; no histidine biosynthesis."
SQ   SEQUENCE   413 AA;  46299 MW;  587DAFE3D440A5AF CRC64;
     MGVIELCNTS SICIGRANPS CCSIERNQRR RIICMASSVP VQEESQQKQR VTGDAFIRPH
     LLKLSPYQPI LPFEVLSTRL GRKPEDIVKL DANENPYGPP PEVIEALGAM KFPYIYPDPE
     SRTLRAALAE DSGLESEYIL AGCGADELID LIMRCVLDPG DMIVDCPPTF TMYEFDAAVN
     GAHVIKVPRN PDFSLDVERI AEVVEHEKPK CIFLTSPNNP DGSIIDDETL LKILDLPILV
     ILDEAYVEFS GMESKMKWVK KHENLIVLRT FSKRAGLAGL RVGYGAFPKS IIEFLWRAKQ
     PYNVSVAAEV AACAALKNPA YLENVKVALV QERERLFNLL KEVPFLDPYP SYSNFILCKV
     TSGMDAKKLK EDLATMGVMI RHYNSKELKG YVRVSVGKPE HTEALMKCLK HFY