ID   HIS8_FRACC              Reviewed;         397 AA.
AC   Q2J8K9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=Francci3_3026;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR   EMBL; CP000249; ABD12383.1; -; Genomic_DNA.
DR   RefSeq; WP_011437411.1; NZ_MSEA01000300.1.
DR   AlphaFoldDB; Q2J8K9; -.
DR   SMR; Q2J8K9; -.
DR   STRING; 106370.Francci3_3026; -.
DR   EnsemblBacteria; ABD12383; ABD12383; Francci3_3026.
DR   KEGG; fra:Francci3_3026; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_11; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 1248286at2; -.
DR   PhylomeDB; Q2J8K9; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..397
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000319759"
FT   MOD_RES         247
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   397 AA;  42037 MW;  52B0F1FA318E67B3 CRC64;
     MIFKAAGSGA EDRPWRPWDA DGLPLRDSLR GLSPYGAPQL DVPVRLNTNE NPHPPSVGLV
     DAIGKAAALA ATEANRYPDR DAEALRADLA YYLTPDAGFG VHTSQVWAAN GSNEILQQLL
     QAFGGPGRVA LGFEPSYSMH RLIALATATE WVAGQRAEDF TLSPAVVTDA IARHRPALVF
     LCSPNNPTGT ALPPEVVAAA CEAVEATGSG MVVVDEAYAE FRRAGVPSTL TLLPRHPRLV
     VTRTMSKAFA LAGARVGYLA AHPAVVDSLY LVRLPYHLSS FTQAVARTAL AHADELLGTV
     EAVKAQRDRI VRELPALGLR LAPSDANFVF FGRFADQRAV WQSLLDAGVL VRDVGLTGWL
     RVTAGLPNEV DAFLGALGRT LTGSVIGADG VISLATA