ID   HIS8_BUCAI              Reviewed;         368 AA.
AC   P57202;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; OrderedLocusNames=BU101;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(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; BA000003; BAB12820.1; -; Genomic_DNA.
DR   RefSeq; NP_239934.1; NC_002528.1.
DR   RefSeq; WP_010895944.1; NC_002528.1.
DR   AlphaFoldDB; P57202; -.
DR   SMR; P57202; -.
DR   STRING; 107806.10038785; -.
DR   EnsemblBacteria; BAB12820; BAB12820; BAB12820.
DR   KEGG; buc:BU101; -.
DR   PATRIC; fig|107806.10.peg.109; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   OMA; IWLNANE; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001806; 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..368
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153329"
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  42123 MW;  86221F9606D4B156 CRC64;
     MTDNVLKLSR KNIKKLIPYQ SARRIGGEHG NILLNANESP VSIFFKLKKK PFNRYPECQP
     SKLISSYAHY VNLSCNQILA TRGADEGIEL LIKAFCEPGK DAIIYCPPTY DMYRINATIA
     GVEIKEIPTI KNTWQLDLLN IKLNLSRVKL IYICNPNNPT GNIFFKKDLI FLLNITLGQA
     LVVIDEAYIE FSPEESMTNY LKDYPNLVVL RTLSKAFALA GIRCGFTLAK KEIIQTLSKV
     ISPYPISIPV SDIAIRSLEK DYVQLMKNRV LDSNNNRIWL INQLKNITCV ETVFESNANY
     VLVKFSMFEK VFETLWNKGI ILRNQNEKTN LKKCIRISMG TRSESLRLIK ELKIFSKKNM
     CQGEMSEK