ID   HIS81_HAEI8             Reviewed;         352 AA.
AC   Q4QN73;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC1 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=NTHI0601;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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   -!- SUBUNIT: Homodimer. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX87524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000057; AAX87524.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041174737.1; NC_007146.2.
DR   AlphaFoldDB; Q4QN73; -.
DR   SMR; Q4QN73; -.
DR   EnsemblBacteria; AAX87524; AAX87524; NTHI0601.
DR   KEGG; hit:NTHI0601; -.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000002525; 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..352
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153370"
FT   MOD_RES         211
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   352 AA;  38891 MW;  FFACC8DB2C4A15C9 CRC64;
     MTITTLSRQN IQALTPYQSA RKLGGNGTIW LNANEYPTSP EFQLSGKDLN RYPEPQPQRV
     VQAYANYAGV STENVLVTRG GDEGIELIIH TFCEPKQDAI LFCPPTYGMY AVSAETAGVL
     SKSVPLTDDF QLNLPEIKNH LNDVKVVFVC SPNNPTGNLL KQSDILDLLQ ITAGKAIVVV
     DEAYIEFCPE ASVINLLKNY PHLAIIRTLS KAFALAGLRC GFVLANPELI DILSKVIAPY
     PIPVPSADLA EQALRPANIA TVQALTQELL SNRQWLAKAL LVLHQVEKVY ESEANYLLIK
     CQNGQAVFKA LWEQGIILRD QNKTLHLQNC IRITVGTRNE CEKVVEAIKE VK