ID   HIS8_THEGJ              Reviewed;         340 AA.
AC   C5A7A4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=TGAM_1614;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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   -!- 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; CP001398; ACS34116.1; -; Genomic_DNA.
DR   RefSeq; WP_015859227.1; NC_012804.1.
DR   AlphaFoldDB; C5A7A4; -.
DR   SMR; C5A7A4; -.
DR   STRING; 593117.TGAM_1614; -.
DR   PaxDb; C5A7A4; -.
DR   EnsemblBacteria; ACS34116; ACS34116; TGAM_1614.
DR   GeneID; 7988508; -.
DR   KEGG; tga:TGAM_1614; -.
DR   PATRIC; fig|593117.10.peg.1618; -.
DR   eggNOG; arCOG04273; Archaea.
DR   HOGENOM; CLU_017584_3_1_2; -.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 69863at2157; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001488; 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; Transferase.
FT   CHAIN           1..340
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_1000213311"
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   340 AA;  38488 MW;  4E5C8C4D39FCCB0A CRC64;
     MISELVKSFQ PYRVVEGNYR IRLDKNENPY DLPGEVKEEI FEELREVSFN RYPHITSMPA
     REAIADFYGV SPDNVAVGNG SDELLSYLVR LFEGNHIVIT PPTFGMYSFY AKLNGVPVVE
     VPLREDFTLD GEAVAEKAKN ARVVFIASPN NPTGNLQPEE EIIRVLETRR PVVLDEAYAE
     FVGKSLWRLI EEYPNLVVLR TFSKAFGMAG IRAGYMLAGE EIVDALYRIK SPFSVGIMTM
     TAIRVALRHA DLMEKTVRKI VEERERMRRK LGELAYPSDA NFLLVRLNAY EELLKRGIVV
     RKLSGRLEGH IRVTVGRRWE NDAFLEAVEE IAGGESVGGL