ID   HIS81_BRADU             Reviewed;         350 AA.
AC   Q89GX0;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN   Name=hisC1; OrderedLocusNames=blr6225;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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   -!- 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; BA000040; BAC51490.1; -; Genomic_DNA.
DR   RefSeq; NP_772865.1; NC_004463.1.
DR   RefSeq; WP_011088965.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89GX0; -.
DR   SMR; Q89GX0; -.
DR   STRING; 224911.27354503; -.
DR   EnsemblBacteria; BAC51490; BAC51490; BAC51490.
DR   GeneID; 64025986; -.
DR   KEGG; bja:blr6225; -.
DR   PATRIC; fig|224911.44.peg.6198; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_0_5; -.
DR   InParanoid; Q89GX0; -.
DR   OMA; FDGYPIL; -.
DR   PhylomeDB; Q89GX0; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000002526; 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..350
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153325"
FT   MOD_RES         209
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   350 AA;  38774 MW;  F51B67F2BE9D7805 CRC64;
     MSRFWSPVVR TLSPYVPGEQ PKQDGVVKLN TNENPYPPSP RVLAAIASAA ERLRLYPDPR
     ATRLREAIAA YCDVAAEQVF VGNGSDEVLA HTFPALLKHD RPLLFPDVTY SFYPVYCRLY
     GVAHEEVPLD AAMRIEIADY RRPSSAILLC NPNAPTGIAL PRDAVAALLA ENPDRLVVVD
     EAYVDFGAES AVPLVAHHDN LLVIQTFSKS RALAGLRVGF AIGQRPLIEA LERVKDSFNS
     YPVDCLAIAG AVAAIEDEAW FLESRTRIIA SRDVLTRDLA QLGFEVLPSL ANFVFARHRR
     RSGADLAAAL RQRGVLVRHF KKPRIEDFLR ITVGTDEQCG RLIEVLRELI