ID   HIS83_RHILO             Reviewed;         369 AA.
AC   Q98B00;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Histidinol-phosphate aminotransferase 3;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 3;
GN   Name=hisC3; OrderedLocusNames=mlr5786;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB52172.1; -; Genomic_DNA.
DR   RefSeq; WP_010913508.1; NC_002678.2.
DR   AlphaFoldDB; Q98B00; -.
DR   SMR; Q98B00; -.
DR   STRING; 266835.14025572; -.
DR   DNASU; 1229045; -.
DR   EnsemblBacteria; BAB52172; BAB52172; BAB52172.
DR   KEGG; mlo:mlr5786; -.
DR   PATRIC; fig|266835.9.peg.4603; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_0_5; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 1248286at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000552; 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; Transferase.
FT   CHAIN           1..369
FT                   /note="Histidinol-phosphate aminotransferase 3"
FT                   /id="PRO_0000153434"
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  40711 MW;  DCB23E0507165570 CRC64;
     MSDAKLQSVL SSLSQVARQL DALPSDTPAP DSSWVKLNTN ENPFPLPEII MQSAIAALER
     QYLYPEDDNI SLREAAANAY SVSMDQVIAG NGSSELLGLV YRAFLTPGDS VAMMSPGFSF
     NRKLATLQGA QFVEIEFSKD HSLPMEQLLF GPAKDAKFIL LANPNNPTGT FVPVADIERL
     VAKSDRLIVL DEAYVDFAPE NGLRLINRYS NLLVLRTFSK SYAAAGVRVG FGFGHPEIIG
     RLRNIQNVFN MNVIGQAVGI SVLAHRAAYA DNHRHIRHER RRVTLALSQL GFSVIPSHAN
     FLLARVPTAQ DGSWWQSAFA RQKILVAVFP DKGLENYIRV SIGTKEQMDA FLRAASRISR
     ILNMSTPPR