ID   HIS8_TOBAC              Reviewed;         413 AA.
AC   O82030;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 90.
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 tabacum (Common 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=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Petit Havana; TISSUE=Leaf;
RX   PubMed=9700073; DOI=10.1023/a:1006007125448;
RA   El Malki F., Frankard V., Jacobs M.;
RT   "Molecular cloning and expression of a cDNA sequence encoding histidinol
RT   phosphate aminotransferase from Nicotiana tabacum.";
RL   Plant Mol. Biol. 37:1013-1022(1998).
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: Mainly expressed in green tissues.
CC       {ECO:0000269|PubMed:9700073}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; Y09204; CAA70403.1; -; mRNA.
DR   PIR; T03270; T03270.
DR   RefSeq; XP_016505697.1; XM_016650211.1.
DR   AlphaFoldDB; O82030; -.
DR   SMR; O82030; -.
DR   STRING; 4097.O82030; -.
DR   GeneID; 107823535; -.
DR   KEGG; nta:107823535; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 693202at2759; -.
DR   BRENDA; 2.6.1.9; 3645.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000084051; Unplaced.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aminotransferase; Chloroplast;
KW   Histidine biosynthesis; Plastid; Pyridoxal phosphate; Reference proteome;
KW   Transferase; 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_0000013449"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  46329 MW;  E645757FF94C7A88 CRC64;
     MGVIELCNTS SICIGRAKPS CCSIERNQRR RIICMASSVP VQEESQQKQR VTGDAFIRPH
     LLKLSPYQPI LPFEVLSTRL GRKPEDIVKL DANENPYGPP PEVIEALGAM KFPYIYPDPE
     SRTLRAALAE DSGLESEYIL AGCGADELID LIMRCVLDPG DMIVDCPPTF TMYEFDAAVN
     GAHVIKVPRN PDFSLDVERI AEVVEHEKPK CIFLTSPNNP DGSIVDDETL LKILDLPILV
     ILDEAYVEFS GMESKMKWVK KHENLIVLRT FSKRAGLAGL RVGYGAFPKS IIEFLWRAKQ
     PYNVSVAAEV AACAALKNPT YLENVKVALV QERERLFNLL KEVPFLDPYP SYSNFILCKV
     TSGMDAKKLK EDLATMGVMI RHYNSKELKG YVRVSVGKPE HTEALMKCLK HFY