ID   HIS8_METFL              Reviewed;         368 AA.
AC   O07131;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; Synonyms=hisH;
OS   Methylobacillus flagellatus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MFK1;
RX   PubMed=9613581; DOI=10.1007/s004380050715;
RA   Serebrijski I., Gomelsky M., Bashkirova E., Chistoserdov A.,
RA   Tsygankov Y.D.;
RT   "Refined genetic map of the obligate methylotroph Methylobacillus
RT   flagellatum.";
RL   Mol. Gen. Genet. 258:133-138(1998).
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U83322; AAB58526.1; -; Genomic_DNA.
DR   AlphaFoldDB; O07131; -.
DR   SMR; O07131; -.
DR   UniPathway; UPA00031; UER00012.
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..368
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153390"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   368 AA;  40134 MW;  C8F47963A732B3AC CRC64;
     MTRLYDFAPS NIRAIAPYQP GKPITELARE MGLKPGVIIK LASNENPLGV SPKAYAAMQD
     ALEDIARYPD GNSFALRDCV CRKFKLQPDQ LVFGNGSNDI LELAARAFLT PGTEAVYAQH
     AFAVYALVTQ ATGASGISVP ARDFGHDLDA MLAAITDKTR LFIANPNNPT GTLLSKPALR
     DFLAKVPRQV LVVLDEAYDE YLAAELKSEA FSWLAEFDNL LISRTLSKAY GLAGLRVGFG
     VTSPGVADLM NRVRQPFNVN SVAQAAAVAA LEDDEFVERS YALNQAGMQQ LTEGLARLGL
     SYIPSYGNFV SFHVAQAAEV YQQLLKRGVI VRPVAAYDMP DYLRVSIGLH AENARFLEVL
     EQILKTRT