ID   HIS8_PYRFU              Reviewed;         338 AA.
AC   Q8TH25;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=PF1665;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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; AE009950; AAL81789.1; -; Genomic_DNA.
DR   RefSeq; WP_011012811.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8TH25; -.
DR   SMR; Q8TH25; -.
DR   STRING; 186497.PF1665; -.
DR   PRIDE; Q8TH25; -.
DR   EnsemblBacteria; AAL81789; AAL81789; PF1665.
DR   GeneID; 41713493; -.
DR   KEGG; pfu:PF1665; -.
DR   PATRIC; fig|186497.12.peg.1731; -.
DR   eggNOG; arCOG04273; Archaea.
DR   HOGENOM; CLU_017584_3_1_2; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 69863at2157; -.
DR   PhylomeDB; Q8TH25; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001013; 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..338
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153503"
FT   MOD_RES         204
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   338 AA;  39086 MW;  A1781B9BB375016C CRC64;
     MIWEEILNFE PYRAVEGNYR IWLDKNESPY DLPPQLKEEI LEELKRIEFN RYPHITSDPL
     REALAEFYGL KKENIAVGNG SDELINYLVK MFKGKYIVVT SPTFGMYSFF AKLHGIPVKD
     IPLKEDFTID GERIAEEGKA ASAIFIASPN NPTGNSQPEN EVLKVLDSGR VVILDEAYSE
     FSGKSFIPKI SEYENLVILR TFSKAFGLAG IRCGYMIANE KIIDALYRIL PPYNLNSLTM
     TVAIKMLEHY DIVKRRIKLI VKERERIRRE FIEYSYPSEA NFLLMKLDAY DYLLKKGIVV
     RKLSGRLEGH IRVTIGKKWE NDELIKALKE FLEECRCG