ID   HIS82_OCEIH             Reviewed;         364 AA.
AC   Q8EQB9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Histidinol-phosphate aminotransferase 2;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN   Name=hisC2; OrderedLocusNames=OB1782;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13738.1; -; Genomic_DNA.
DR   RefSeq; WP_011066181.1; NC_004193.1.
DR   AlphaFoldDB; Q8EQB9; -.
DR   SMR; Q8EQB9; -.
DR   STRING; 221109.22777466; -.
DR   EnsemblBacteria; BAC13738; BAC13738; BAC13738.
DR   KEGG; oih:OB1782; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_9; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 1248286at2; -.
DR   PhylomeDB; Q8EQB9; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000822; 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..364
FT                   /note="Histidinol-phosphate aminotransferase 2"
FT                   /id="PRO_0000153408"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  41660 MW;  CF6D0E7FB6A8FD0F CRC64;
     MQGKEILKQL SPYKQGKQIK DIQKDYQLDY IVKLASNENP YGYSKQVNEA LSTENFDFHI
     YPDGYTSDLR TDLTQKLNID ESEIIFGSGS EEIIQLLCRS YIIPGSNVVM ATPTFPQYKH
     YSLIENAEIK EIPTDKEGYH QLDKMLGSID DHTAIVWLCT PNNPTGAAFS KEELITFLDN
     CPKEVLVVLD EAYYEYLHSD KDLDALQLRF TYSNVIVLRT FSKAYGLAGL RIGYGIANST
     IIETLDKVRG PFNTNSVAQK AASYALKDQE FIQHTNQENY KNLTEFQHFL QRLGWGYYDS
     EANFLLVKTP ISGMDVYEYL LRFGFIVRPG ELLGIPKTVR VTIGKEQDMK ELQKVLEQFD
     HELG