ID   HIS8_CAMC5              Reviewed;         365 AA.
AC   A7H084;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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};
GN   OrderedLocusNames=Ccur92_15720; ORFNames=CCV52592_1667;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-2007) 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; 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; CP000767; EAU01005.1; -; Genomic_DNA.
DR   RefSeq; WP_011992672.1; NC_009715.2.
DR   AlphaFoldDB; A7H084; -.
DR   SMR; A7H084; -.
DR   STRING; 360105.CCV52592_1667; -.
DR   PRIDE; A7H084; -.
DR   EnsemblBacteria; EAU01005; EAU01005; CCV52592_1667.
DR   KEGG; ccv:CCV52592_1667; -.
DR   HOGENOM; CLU_017584_3_3_7; -.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 1248286at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000006380; 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; Reference proteome; Transferase.
FT   CHAIN           1..365
FT                   /note="Histidinol-phosphate aminotransferase"
FT                   /id="PRO_1000063464"
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   365 AA;  41149 MW;  C7A4A932FCF82D26 CRC64;
     MKFNENLAGL VNYEAGKPIE LVVREFGIEA KDVIKLASNE NPFGTSPHVV EAIKSAASNA
     FLYPDDSYFE LKEALGAKFG VGTKNIIIGS GSDQIIEFCL HAKANPQSAV LMAGVTFAMY
     EIYAKQVGAK IYRTRSQEHD LAEFLEIYEA HKDEISVIFL CLPNNPLGEC LDTKEVYEFL
     KRIDEDVLVV LDCAYNEFAK FKDARKGIES SEILKFKNVI YLGTFSKAYG LGGMRVGYGI
     AKESIISELC KLRAPFNITT LSLKAAIEAL KDEEFVTKTL ENNLKQMARY EAFAREADIE
     FIPSYTNFIT FKFDKQSASE ISQNMLKKGI ILRDLKSYKL NAFRITIGQS WQNDRVFEEL
     KQNLK