ID   HIS83_BURL3             Reviewed;         370 AA.
AC   Q39M27;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Histidinol-phosphate aminotransferase 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC3 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=Bcep18194_C7445;
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=482957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; 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; CP000150; ABB06489.1; -; Genomic_DNA.
DR   RefSeq; WP_011350132.1; NC_007509.1.
DR   AlphaFoldDB; Q39M27; -.
DR   SMR; Q39M27; -.
DR   EnsemblBacteria; ABB06489; ABB06489; Bcep18194_C7445.
DR   GeneID; 45092813; -.
DR   KEGG; bur:Bcep18194_C7445; -.
DR   PATRIC; fig|482957.22.peg.8042; -.
DR   HOGENOM; CLU_017584_3_1_4; -.
DR   OMA; FPPLNDW; -.
DR   OrthoDB; 1248286at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000002705; Chromosome 3.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..370
FT                   /note="Histidinol-phosphate aminotransferase 3"
FT                   /id="PRO_0000230210"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   370 AA;  40073 MW;  D40D94C1C3418EF2 CRC64;
     MQQPWKAVAL SDLPLREDLK LQHAYGAPQL DVPVCLNVNE NPYPPSPALV ERIATAVADA
     ARAANRYPDR DFAALRSHLA AYLTHDTGVT VDASSVWAAN GSNEVIQQIL QAFGGPGRSA
     LAFTPAYPMY DEYCRTTFTR LHTLPRTEDF ALDLNQALDS IRAHQPGVVL LTSPNNPTGT
     ALPIDDIRAI LDAAPGVVVV DEAYAEFRRH GVPSAVTLLP AYPRLIVTRT LSKAFKFAGG
     RVGYCACAPA IVEALKLVRL PYHLSAFTQA AACAALVARD EMLSQVEAIK AERDSTVDWL
     RGLGLTVADS DANFVMFGEF ADRHRIWSGL LRRGVLIRES GPPPYLRVSI GTGAEMAAFR
     AALLDVMALE