ID   HIS8_BURM1              Reviewed;         364 AA.
AC   Q845V2; A9AE02; B3D448;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Histidinol-phosphate aminotransferase {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 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023};
GN   OrderedLocusNames=Bmul_0329, BMULJ_02925;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12754231; DOI=10.1128/jb.185.11.3333-3343.2003;
RA   Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.;
RT   "Distribution and organization of auxotrophic genes on the multichromosomal
RT   genome of Burkholderia multivorans ATCC 17616.";
RL   J. Bacteriol. 185:3333-3343(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG44810.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB091436; BAC65271.1; -; Genomic_DNA.
DR   EMBL; CP000868; ABX14024.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44810.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q845V2; -.
DR   SMR; Q845V2; -.
DR   STRING; 395019.Bmul_0329; -.
DR   EnsemblBacteria; BAG44810; BAG44810; BMULJ_02925.
DR   KEGG; bmj:BMULJ_02925; -.
DR   KEGG; bmu:Bmul_0329; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_4; -.
DR   OMA; YPDMACT; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000008815; 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; 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; Reference proteome; Transferase.
FT   CHAIN           1..364
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153337"
FT   MOD_RES         224
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   364 AA;  39230 MW;  9142B0201023EEAB CRC64;
     MHAGLPTMTT PQDIIRRDVL AMTSYPVPDA SGFVKLDAME NPYPLPEPLA AALGERLARV
     ALNRYPAPRP AALLDKLRHA MGVPGTCDVL LGNGSDEIIS MISVACAKPG AKVLAPVPGF
     VMYELSARFA QLDFVGVPLK ADLTLDVDAM LAAIAEHRPA IVYLAYPNNP TGTLYDDADI
     ERILRAATHS LIVIDEAYQP FAQHSWLPRA GEFDNVVVMR TVSKLGLAGI RLGYLVGRPA
     WLNEFDKVRP PYNINVLTQA TADFLLDHLD VLDAQAAELR AERARLAQAV AALPGATVFP
     SAGNFLLVRV PDAAAVFDAL LTERVLVKNV SKMHPLLAEC VRLTVGSPDE NARLLAALKL
     ALPD