ID   HIS8_PSEST              Reviewed;         366 AA.
AC   Q9RI00;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
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}; Synonyms=hisHB;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 10701 / JCM 21571 / JM300;
RX   PubMed=10368439; DOI=10.1007/pl00006523;
RA   Xie G., Bonner C.A., Jensen R.A.;
RT   "A probable mixed-function supraoperon in Pseudomonas exhibits gene
RT   organization features of both intergenomic conservation and gene
RT   shuffling.";
RL   J. Mol. Evol. 49:108-121(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   -!- 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}.
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DR   EMBL; AF038578; AAD47361.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RI00; -.
DR   SMR; Q9RI00; -.
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; 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..366
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153422"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   366 AA;  39700 MW;  397506C7409EDB6F CRC64;
     MSADFLALAV PGVQKLSPYV TGKPIDELAR ELGIEPARIV KLASNENPLG PNPRVLEAVR
     GELSELTRYP DGSGFRLKAK LAERFGLKSE QITLGNGSND IIDLVARCCG AGPNAVFSAH
     AFAAYPLCTQ AAGAESRVVP AVDYGHDLDG MLKAIDEQTA VIFIANPNNP TGNLVRAQAL
     ESFLDRVPER VLVVLDEAYI EFYRGTNCQR LNYLVRYPNL LVSRTLSKVY GLAGLRVGYS
     ASSPQIADVL NRVRQPFNVN SLALVAACAG WMTSSIWLKG GGWIAPVWEL EQGLAELRLK
     WIPSRGNFLA VDLGRDAAPI NAGLLRDGVI VRPIAGYDCP TFLRVSIGTE QENARFLEAL
     RVVLDQ