ID   HIS82_MANSM             Reviewed;         350 AA.
AC   Q65RB2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 115.
DE   RecName: Full=Histidinol-phosphate aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC2 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=MS1891;
OS   Mannheimia succiniciproducens (strain KCTC 0769BP / MBEL55E).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 0769BP / MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidinol phosphate + 2-oxoglutarate = 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR   EMBL; AE016827; AAU38498.1; -; Genomic_DNA.
DR   RefSeq; WP_011201051.1; NC_006300.1.
DR   AlphaFoldDB; Q65RB2; -.
DR   SMR; Q65RB2; -.
DR   STRING; 221988.MS1891; -.
DR   KEGG; msu:MS1891; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   OrthoDB; 9813612at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000607; Chromosome.
DR   GO; GO:0004400; F:L-histidinol-phosphate:2-oxoglutarate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
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   NCBIfam; TIGR01141; hisC; 1.
DR   PANTHER; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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 2"
FT                   /id="PRO_0000153389"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   350 AA;  38386 MW;  B9BB86DAFAF6B9E3 CRC64;
     MSISQLSRKN VQALTPYQSA RRLGGNGDVW LNANEYPTSP DFNLSERIFN RYPEPQPEAV
     IKGYAAYADV KPENVIVTRG GDESIELLIK GFCEPEDKVL YCPPTYGMYA VSAETLGIAT
     KTVPLTEDFQ LDLPEIEKNL AGVKVIFVCS PNNPTGNVLN QADLIRLLDI TAGSAIVVVD
     EAYIEFSPET SMIKQLGNYP HLAIIRTLSK AFALAGLRCG FTLANPELIG VLQKVIAPYP
     LPVPVSDIAA QALQPQGVAQ MKMRVADVLA NRAWLIGELK QIPSVVKIFA TEANYVLVKF
     QDGEKVFNAL WEKGIILRDQ HKAFGLKNCI RISIGTRAEL EKTVVALKLA
//