HIS8_BACNA
ID HIS8_BACNA Reviewed; 360 AA.
AC Q8KZ92;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 68.
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 Bacillus subtilis subsp. natto.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=86029;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OK2;
RA Murayama R., Nanamiya H., Kawamura F.;
RT "Genetic analysis of trpA and hisC genes in Bacillus subtilis natto OK2.";
RL Submitted (SEP-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; AB091253; BAC11847.1; -; Genomic_DNA.
DR RefSeq; WP_014480119.1; NZ_SJSU01000007.1.
DR AlphaFoldDB; Q8KZ92; -.
DR SMR; Q8KZ92; -.
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..360
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153309"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 360 AA; 40050 MW; 8978AB35611DF974 CRC64;
MRIKEHLKQL KPYQPGKPIE AVKSEYGLDK VVKLASNENP YGCSEAAKEA LHHEIQQLAL
YPDGYSAALR TRLSKHLNVS ETSLIFGNGS DEIIQIICRA FLNNKTNTIT AAPTFPQYKH
NAVIEGAEVR EIALRPDGSH DLDAMLEAID EQTQVVWICS PNNPTGTYTS EGELLAFLER
VPSRVLVVLD EAYYEYVTAE DYPETVPLLS KYSNLMILRT FSKAYGLAAL RVGYGIADEN
LIRQIEPARE PFNTSRLGQA AAIAALDDQA FIASCVEQNN AGLQQYYDFA KTHGLKCYPS
QTNFVLIDFK RPADELFQAL LEKGYIVRSG NALGFPTSLR ITIGTKEQNE EILAILAEIL