ID   HIS8_METM5              Reviewed;         371 AA.
AC   A4FWW1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=MmarC5_0374;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO34690.1; -; Genomic_DNA.
DR   RefSeq; WP_011868145.1; NC_009135.1.
DR   AlphaFoldDB; A4FWW1; -.
DR   SMR; A4FWW1; -.
DR   STRING; 402880.MmarC5_0374; -.
DR   EnsemblBacteria; ABO34690; ABO34690; MmarC5_0374.
DR   GeneID; 4928519; -.
DR   KEGG; mmq:MmarC5_0374; -.
DR   eggNOG; arCOG04273; Archaea.
DR   HOGENOM; CLU_017584_3_3_2; -.
DR   OMA; IWLNANE; -.
DR   OrthoDB; 69863at2157; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000253; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..371
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000319798"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   371 AA;  42232 MW;  F01906BAD8510EA9 CRC64;
     MSIDDKVRAI VKEFKAYVPG KSKEEIARNY GIDPEKIIKL GSNENPWGCS PKIAEKLMNE
     VSNLHQYPQP INPELMDEIS KFTKMPTENI IVGGDGADEV IDNIMRILID EGDEVIIPIP
     TFTQYAISAK IHGANIKWAK FDEENGFKLD VESVLNNITE KTKVIFLCTP NNPTGNVIPT
     EDIKKIVEST DALVMIDHAY IEYSKGEYDL TNWALKYDNV LVLRTFSKVF GLAGQRVGFG
     VTSKKIVDYM MRIKPIFSLT RASQVSAITA LQDKEFFDRC LKEGIESREQ IYNGLKKFKQ
     LEVYPTEANY MLVKVKNGMN SSEFCEALLK KGVIVRDCYS FEGLEPYYFR ISIGTFEENE
     RFLKIMSEIV E