ID   HIS8_XANC5              Reviewed;         363 AA.
AC   Q3BUF6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
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}; OrderedLocusNames=XCV1876;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(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}.
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DR   EMBL; AM039952; CAJ23553.1; -; Genomic_DNA.
DR   RefSeq; WP_011347186.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BUF6; -.
DR   SMR; Q3BUF6; -.
DR   STRING; 456327.BJD11_13045; -.
DR   EnsemblBacteria; CAJ23553; CAJ23553; XCV1876.
DR   KEGG; xcv:XCV1876; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_1_6; -.
DR   OMA; IWLNANE; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000007069; 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; 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..363
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_0000153483"
FT   MOD_RES         218
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   363 AA;  38623 MW;  C1370E848527FB10 CRC64;
     MSASSILDLV REDLRAFAGY SSARTSALQG DVWLNANESA WANPADPDAS TRRYPDPQPK
     GLRSALAALY GCAPEQLLIG RGSDEAIDLL VRGLCVPGRD AVLVTPPVFG MYAVCARLQN
     APLVDVPLVD GPDGFRADIP AIVARALASN AKLVFLCSPS NPAGSAIALD QIEQALQALQ
     GKALVVVDEA YGEFSDVPSA VGLLGRYDNL AVLRTLSKAH ALAAARIGTL IANAELIALL
     RRCQAPYPVP TPCAAMAEQA LSAPALEVTR RRIAEVRSER ERVHEALAQL AGVRQVYPSQ
     GNFLLVRFDD AEAAFQALLD AGVVVRDQRA VPRLADALRI TLGTHEQNQR VLSALQRTQE
     AVA