ID   HIS8_CANMA              Reviewed;         389 AA.
AC   P56099;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=HIS5;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2697466; DOI=10.1007/bf00422112;
RA   Hikijii T., Ohkuma M., Takagi M., Yano K.;
RT   "An improved host-vector system for Candida maltosa using a gene isolated
RT   from its genome that complements the his5 mutation of Saccharomyces
RT   cerevisiae.";
RL   Curr. Genet. 16:261-266(1989).
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   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X17310; CAA35189.1; -; Genomic_DNA.
DR   PIR; A48329; A48329.
DR   AlphaFoldDB; P56099; -.
DR   SMR; P56099; -.
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   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; Transferase.
FT   CHAIN           1..389
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153507"
FT   MOD_RES         233
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  43392 MW;  282D1E52D232B9EA CRC64;
     MFDIKSIIRP NILTLEPYRC ARDDFKTGIL LDANENTHGP AIPTPDETEL ALELNRYPDP
     HQLELKQQVI DFREKHPNKY TKEKLSVENL CLGVGSDESI DMLLRCVCVP GKDKMLICPP
     TYGMYSICAT VNDVVIEKVP LTVPDFQIDI PAILSKVKSD PNIKLLYLTS PGNPTGKLIN
     VDSIITLLEE LLNCWQGLIV VDEAYIDFTE PGSSMSTLVN QYPNLVVLQT LSKSFGLAGI
     RLGITFCSKE LSWYLNAMKY PYNISSLTSN VALKATKQGL EIMENYVSKI TEQRDIVLQK
     LLSLKYVGRN IGGLDSNFVL VEVLDKQGNP SNEVAKQLYN TLATGKSIVV RFRGSELNCV
     GGLRISIGTE EENKQLLEQF EAVLNDINQ