ID   HIS81_RHILO             Reviewed;         367 AA.
AC   Q987C8;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=mll7105;
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; BAB53275.1; -; Genomic_DNA.
DR   RefSeq; WP_010914582.1; NC_002678.2.
DR   AlphaFoldDB; Q987C8; -.
DR   SMR; Q987C8; -.
DR   STRING; 266835.14026679; -.
DR   EnsemblBacteria; BAB53275; BAB53275; BAB53275.
DR   KEGG; mlo:mll7105; -.
DR   PATRIC; fig|266835.9.peg.5667; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_5; -.
DR   OMA; IMMGPGS; -.
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..367
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153432"
FT   MOD_RES         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  39889 MW;  05E2F4E31307DB34 CRC64;
     MSKASDMVRT EVTRPSPYNS GLTITEVMQR YAPARIAKLG SNENPLGPSP TLATMLQAGA
     EMFRLYPDPA GRELRQAIAA KYGFGEDQII LGNGSEDLLS VISRAVLRPG DSVVTLYPSF
     PLHEDYATLM GASVKRVTVN DDLTINADAL IDAVRERPRM LLFSNPMNPV GSWLSAGDLS
     KVLDAVSDET LIVVDEAYAE YAEGDDYASS LPDLCERDQP WIVLRTFSKA FGLAGLRIGF
     GIVGDPELRA LLDRVRTPFN ANGMAQAAAL AALADEEHLA KVVALAKAER TQVESLLRNM
     GFDVAPSRGN FLFFNCRQNA SAFAEGLLRE GVIVKPWKQE GFDSYVRVSI GSPAENDHFM
     AALSQLL