ID   HIS8_ACEPA              Reviewed;         356 AA.
AC   P45358;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
GN   Name=hisC; Synonyms=his1;
OS   Acetobacter pasteurianus (Acetobacter turbidans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCI 1452;
RA   Takemura H., Horinouchi S., Beppu T.;
RT   "Suppression of an ethanol-sensitive mutation of Acetobacter pasteurianus
RT   by overexpression of the his1 gene encoding histidinol phosphate
RT   aminotransferase.";
RL   J. Ferment. Bioeng. 76:224-228(1993).
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; D14440; BAA03332.1; -; Genomic_DNA.
DR   PIR; I39488; I39488.
DR   AlphaFoldDB; P45358; -.
DR   SMR; P45358; -.
DR   STRING; 940282.CADQ01000004_gene266; -.
DR   eggNOG; COG0079; Bacteria.
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..356
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153290"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  39136 MW;  8926199C5242DF51 CRC64;
     MSRFWSPLVH KLTPYVPGEQ PKMTDLIKLN TNESPYGPSP RALEAIRAAD NDTLRLYPDP
     EALALRKALG ARIGLGPEYV FVGNGSDEVL AHAFQAFFAH GEPLLFPDVT YSFYKVYCGL
     YSLPFRNVPL TDDMQVNVAD YAGPCSGVVV ANPNAPTGIA LDLADVRKLL ELQPNRVVLI
     DEAYVDFGAE SAVSLIKEYP NLLVVQTFSK SRALAGLRVG FAFGQPELIE GLVRIKDSFN
     SYPLDRLAQV GATAAVEDEA WLATSVQKVM ASRTVLTEGL QKLGFDVLPS KANFVYTRHP
     NRNAAELATQ LRERAIIVRH LRGERTAAWL RITVGTDQQC ETLLSALRDI LCSNSL