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HIS8_THIRO
ID   HIS8_THIRO              Reviewed;         189 AA.
AC   Q9L6I2;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Histidinol-phosphate aminotransferase;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase;
DE   Flags: Fragment;
GN   Name=hisC;
OS   Thiocapsa roseopersicina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=1058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Milles J., Kappler U., Truper H.G., Dahl C.;
RT   "Genes for putative enzymes of histidine biosynthesis from the phototrophic
RT   sulfur bacterium Thiocapsa roseopersicina.";
RL   Submitted (FEB-2000) 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;
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; AF235018; AAF44660.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L6I2; -.
DR   SMR; Q9L6I2; -.
DR   UniPathway; UPA00031; UER00012.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..>189
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153473"
FT   NON_TER         189
SQ   SEQUENCE   189 AA;  20739 MW;  924246178BFE61C4 CRC64;
     MIDLITQLIR PDIRALSAYH VPDPAGLIKL DAMENPYGWP DTLKAEWLEG MHDLALNRYP
     DPQGTAVQAA LRQAMGIPSD MGLLLGNGSD ELIQMLAIAV AQPGRKVLSL DPGFVMYRMI
     ACFAGMDYVG VPLRSDDFSI DLPVMLDAIE REQPALIYLA YPNNPTGNRF DSDDMVRIIE
     AAPGLVIVD
 
 
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