ID   B3R366_CUPTR            Unreviewed;       377 AA.
AC   B3R366;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 109.
DE   RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023};
DE            EC=2.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01023};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|HAMAP-Rule:MF_01023};
GN   Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023,
GN   ECO:0000313|EMBL:CAQ68746.1};
GN   OrderedLocusNames=RALTA_A0774 {ECO:0000313|EMBL:CAQ68746.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ68746.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ68746.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidinol phosphate + 2-oxoglutarate = 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         Evidence={ECO:0000256|ARBA:ARBA00047481, ECO:0000256|HAMAP-
CC         Rule:MF_01023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         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:0000256|ARBA:ARBA00005011, ECO:0000256|HAMAP-Rule:MF_01023}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01023}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000256|ARBA:ARBA00007970, ECO:0000256|HAMAP-
CC       Rule:MF_01023}.
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DR   EMBL; CU633749; CAQ68746.1; -; Genomic_DNA.
DR   RefSeq; WP_012352083.1; NC_010528.1.
DR   AlphaFoldDB; B3R366; -.
DR   GeneID; 29761708; -.
DR   KEGG; cti:RALTA_A0774; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_4; -.
DR   BioCyc; CTAI977880:RALTA_RS03735-MONOMER; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001692; Chromosome 1.
DR   GO; GO:0004400; F:L-histidinol-phosphate:2-oxoglutarate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:L-histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR050106; HistidinolP_aminotransfase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01141; hisC; 1.
DR   PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_01023}; Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_01023}; Reference proteome {ECO:0000313|Proteomes:UP000001692};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01023}.
FT   DOMAIN          45..366
FT                   /note="Aminotransferase class I/classII large"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         236
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   377 AA;  40419 MW;  BDC524AB7ADB0C43 CRC64;
     MAEQGKQGGA TTVFGPDYVR AISPYVAGKP ISEVAREFGL DEAGIVKLAS NENPLGMPDS
     ARAAVAAAVA ELGRYPDANG FALKGALSAR FGVPAEWLTL GNGSNDILEL AAHALVEPGQ
     SIVYAEYSFA VYALATQEIG ARAIEVPARD YGHDLDAMAA AIAPDTRLVF IANPNNPTGT
     FLPAAQLEAF LQRVPRHVVV VLDEAYNEYL DADQQYDAIA WVRRYPNLLV SRTFSKAYGL
     AGLRIGYAVA QPELTDLLNR IRQPFNVNSV AQAAAMAALA DTGFLRRSAE LNRDGKRQLT
     EAFDRLGLEY VPSSGNFVLV RVGDDDGAGA HVNLALLRQG VIVRPVGNYN LPRWLRVTIG
     LPEENAAFIA ALERALA
//