ID   HIS8_MYCSM              Reviewed;         219 AA.
AC   P28735;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
DE   Flags: Fragment;
GN   Name=hisC;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX   PubMed=1435262; DOI=10.1111/j.1365-2958.1992.tb01468.x;
RA   Hinshelwood S., Stoker N.G.;
RT   "Cloning of mycobacterial histidine synthesis genes by complementation of a
RT   Mycobacterium smegmatis auxotroph.";
RL   Mol. Microbiol. 6:2887-2895(1992).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X65542; CAA46510.1; -; Genomic_DNA.
DR   PIR; S26210; S26210.
DR   AlphaFoldDB; P28735; -.
DR   SMR; P28735; -.
DR   UniPathway; UPA00031; UER00012.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..>219
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153396"
FT   NON_TER         219
SQ   SEQUENCE   219 AA;  23463 MW;  431F39B371CEB4A8 CRC64;
     MSADKVTLAD LPLRDNLRGK SPYGAPQLQV PVRLNTNENP HPPSKALVDD VAASVREAAA
     ELHRYPDRDA VALRTDLAAY LTAATGVRLG VENLWAANGS NEILQQLLQA FGGPGRTAIG
     FVPSYSMHPI ISDGTQTEWL QASRAEDFGL DIDVAVSAVT ERKPDVVFVT SPNNPSGQSV
     PLDDLRRVLD AMQGGILIVD EAYGEFSSQP SAVALLDDY