ID   HIS81_PASMU             Reviewed;         351 AA.
AC   Q9CLM3;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN   Name=hisC1; Synonyms=hisC; OrderedLocusNames=PM1199;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03283.1; -; Genomic_DNA.
DR   RefSeq; WP_010907066.1; NC_002663.1.
DR   AlphaFoldDB; Q9CLM3; -.
DR   SMR; Q9CLM3; -.
DR   STRING; 747.DR93_767; -.
DR   PRIDE; Q9CLM3; -.
DR   EnsemblBacteria; AAK03283; AAK03283; PM1199.
DR   KEGG; pmu:PM1199; -.
DR   PATRIC; fig|272843.6.peg.1210; -.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   OMA; IWLNANE; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000809; 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..351
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153410"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  38981 MW;  757529C3656BDF5B CRC64;
     MSISSLSRKN IQALTPYQSA RRLGGKGDIW LNANEYPTSP DFNLTHRTFN RYPEPQPQAV
     IEGYANYVGV TPENVLVSRG GDESIELIIR AFCEAEDSIL YCPPTYGMYA VSAETCGIAL
     KTVPLTADFQ LNLPEIERQL TGVKVVFVCS PNNPTGTLVN RTDLLALLEM TRNKAIVVVD
     EAYIEFCPQA TMVTELKNYP HLAIIRTLSK AFALAGLRCG FTLANKDLIE VLQKVIAPYP
     LPVPVADLAA QALQPAGLQA MQQRVQEILQ NRTALEADLR SLPCVENVFQ SDGNYLLVKF
     KDGQKIFKTL WDQGIILRNQ HSALMLENCI RITIGTAEEN RRVIEAIRKI A