ID   HIS8_MYCPA              Reviewed;         398 AA.
AC   P61001;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 111.
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}; OrderedLocusNames=MAP_1294;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS03611.1; -; Genomic_DNA.
DR   RefSeq; WP_003876206.1; NC_002944.2.
DR   AlphaFoldDB; P61001; -.
DR   SMR; P61001; -.
DR   STRING; 262316.MAP_1294; -.
DR   EnsemblBacteria; AAS03611; AAS03611; MAP_1294.
DR   KEGG; mpa:MAP_1294; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_11; -.
DR   OMA; IWLNANE; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000580; 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..398
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153395"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         234
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   398 AA;  42212 MW;  FBD36528B9343FC7 CRC64;
     MTGQRATPQP TLDDLPLRDD LRGKSPYGAP QLAVPVRLNT NENPHPPSRA LVDDVVRSVA
     RAAADLHRYP DRDAVQLRSD LARYLTAQTG VQLGVENLWA ANGSNEILQQ LLQAFGGPGR
     SAIGFVPSYS MHPIISDGTR TEWLQAARAD DFSLDVDAAV AAVTERTPDV VFVASPNNPS
     GQSVSLSGLR RLLDAAPGIV IVDEAYGEFS SQPSAVQLVG EYPTKLVVTR TMSKAFAFAG
     GRLGYLIATP AVIEAMLLVR LPYHLSSVTQ AAARAALRHA DDTLGSVAAL IAERERVSTA
     LTGMGFRVIP SDANFVLFGE FTDAPASWQR YLDAGVLIRD VGIPGYLRAT TGLAEENDAF
     LRASAQLAAT ELAPVNVGAI ANAAEPRAAG RDRVLGAP