HIS8_CAMJJ
ID HIS8_CAMJJ Reviewed; 364 AA.
AC A1VY36;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=CJJ81176_0339;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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; CP000538; EAQ73354.1; -; Genomic_DNA.
DR RefSeq; WP_002868749.1; NC_008787.1.
DR AlphaFoldDB; A1VY36; -.
DR SMR; A1VY36; -.
DR STRING; 354242.CJJ81176_0339; -.
DR PRIDE; A1VY36; -.
DR EnsemblBacteria; EAQ73354; EAQ73354; CJJ81176_0339.
DR KEGG; cjj:CJJ81176_0339; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_7; -.
DR OMA; YPDMACT; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000000646; 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..364
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000063468"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 364 AA; 41350 MW; 6269B8ED1C85F5D4 CRC64;
MKFNEFLNHL SNYEPGKDIE VIAKEYGVKE VIKLASNENP FGTPPKAIEC LRQNANKAHL
YPDDSMIELK STLAQKYKVQ NENIIIGAGS DQVIEFAIHA KLNSKNAFLQ AGVTFAMYEI
YAKQCGAKCY KTQSITHDLN EFKKLYEAHK DEIKLIFLCL PNNPLGECLD ASEVTKFIKG
VDEDCLVVID AAYNEFASFK DSKKHLEPCE LIKEFDNVLY LGTFSKLYGL GGLRIGYGIA
NANIISAFYK LRAPFNVSNL ALKAAVAAIN DDEFAKKTLE NNFSQMELYK EFAKKYDIKI
IDSYTNFITY FFDEKNSTDL SEKLLKKGII IRNLKSYGLN AIRITIGTSY ENEKFFTEFD
KILR
