ID   HIS82_PASMU             Reviewed;         365 AA.
AC   Q9CMI7;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Histidinol-phosphate aminotransferase 2;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN   Name=hisC2; Synonyms=hisH_1; OrderedLocusNames=PM0838;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK02922.1; -; Genomic_DNA.
DR   RefSeq; WP_010906872.1; NC_002663.1.
DR   AlphaFoldDB; Q9CMI7; -.
DR   SMR; Q9CMI7; -.
DR   STRING; 747.DR93_1678; -.
DR   EnsemblBacteria; AAK02922; AAK02922; PM0838.
DR   KEGG; pmu:PM0838; -.
DR   PATRIC; fig|272843.6.peg.849; -.
DR   HOGENOM; CLU_017584_3_3_6; -.
DR   OMA; NYHVAGF; -.
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..365
FT                   /note="Histidinol-phosphate aminotransferase 2"
FT                   /id="PRO_0000153411"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  40250 MW;  F2049EDE8ABCAA85 CRC64;
     MQYINIVNEG VKQLHPYQAG KPIEELEREL GITNIIKLAS NENPFGLPDS AKQAILAELD
     NLTRYPDSNG FYFKQTVAKK FGLSPEQITL GNGSNDLLEL VAHTFANEQD EILFSQYAFI
     VYPLVTQAIN AKKVEIPAKN YGADLDGFLQ AISDKTKLIY LANPNNPTGT FLSAGEISQF
     LNQVPAHVIV VLDEAYTEFT LPEERVDSFT LLKKHSNLVI CRTLSKAYGL AGLRIGYAVS
     SAEIADLFNR VRQPFNCNSL ALAAATAVLH DDAFIAKVAE NNRQGLKLLE DFFTAKGLNY
     IPSKGNFVML DVNQPALPIY QALLQKGVIV RPIAGYGLPN HLRISIGLPE ENQRFLLALN
     EVLGL