HIS8_BUCSC
ID HIS8_BUCSC Reviewed; 359 AA.
AC Q84I51;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 75.
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};
OS Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moran N.A., Mira A.;
RT "Levels of selection on genes of mutualistic endosymbionts.";
RL Submitted (JAN-2002) 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; AF465532; AAO33047.1; -; Genomic_DNA.
DR RefSeq; WP_075473886.1; NZ_CP011299.1.
DR AlphaFoldDB; Q84I51; -.
DR SMR; Q84I51; -.
DR STRING; 118110.XW81_00475; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
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; 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; Transferase.
FT CHAIN 1..359
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153334"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 359 AA; 41221 MW; 2DC2EF6954C37658 CRC64;
MNIKQLVRKN IQELQPYQSA RTIGGKGDIW LNANECPTFN RLKLENIFLN RYPECQPREL
LLRYSSYIGL DKKNILITRG SDEAIELLIK TFCEPQCDRI VFCPPTYDMY NVSANIMGVE
CLQIPLLNHS WQLDLKVIKK CINNFKLIYL CNPNNPTGSL INFRDVLALL KMTYGKSLVI
IDEAYIEFSP MNSLVNLISQ YSNLVVLRTL SKAFSLAGLR CGFVLANFSV IKFLLKVINP
YPISTPTSSI AIQFLSNINI SKMQDRVFSL ILNRCWLINE LKLISNCIDH IFYSASNYVL
VRFRNSNKVF HELSNQGIIV RDQSKKINLK NCIRISIGTS QECLKVIHAI RKIDCLYVN