ID   HIS81_BURPS             Reviewed;         356 AA.
AC   Q63XM1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC1 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=BPSL0518;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH34508.1; -; Genomic_DNA.
DR   RefSeq; WP_004530940.1; NZ_CP009538.1.
DR   RefSeq; YP_107144.1; NC_006350.1.
DR   AlphaFoldDB; Q63XM1; -.
DR   SMR; Q63XM1; -.
DR   STRING; 272560.BPSL0518; -.
DR   EnsemblBacteria; CAH34508; CAH34508; BPSL0518.
DR   KEGG; bps:BPSL0518; -.
DR   PATRIC; fig|272560.51.peg.1129; -.
DR   eggNOG; COG0079; Bacteria.
DR   OMA; FDGYPIL; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000605; Chromosome 1.
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..356
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153338"
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   356 AA;  39286 MW;  2552F2D2AFA5C806 CRC64;
     MSRYWSDIVR QLEPYVPGEQ PALAHPVKLN TNENPYPPSP RALDAIRREL GDTGEALRRY
     PDPVARRLRE TVAAYHGIAP EQVFAGNGSD EVLAHAFQAL LQHDRPLRFP DITYSFYPTY
     ARLYRVAYET VPLADDFSIV VDDYLDDAGC VLFPNPNAPT GRALPLADIE RIVAANPSSV
     VVIDEAYVDF GAESAVSLIA RYPNLLVVHT VSKARSLAGM RVGFAFGDAA LIDALTRVKD
     SFNSYPLDRL AQVATQASYE DEAWFQATRK QVIASRERLV GALAALGFDV VPSAANFVFA
     RPRSHDAATL AAQLKQREIF VRHFKLPRID QHLRITVGSD AECDALVAAL RELLAA