HIS8_CAMJE
ID HIS8_CAMJE Reviewed; 364 AA.
AC Q9PII2; Q0PBJ2;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
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}; OrderedLocusNames=Cj0317;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34468.1; -; Genomic_DNA.
DR PIR; A81451; A81451.
DR RefSeq; WP_002858650.1; NC_002163.1.
DR RefSeq; YP_002343755.1; NC_002163.1.
DR PDB; 3GET; X-ray; 2.01 A; A/B=1-364.
DR PDBsum; 3GET; -.
DR AlphaFoldDB; Q9PII2; -.
DR SMR; Q9PII2; -.
DR STRING; 192222.Cj0317; -.
DR PaxDb; Q9PII2; -.
DR PRIDE; Q9PII2; -.
DR EnsemblBacteria; CAL34468; CAL34468; Cj0317.
DR GeneID; 904641; -.
DR KEGG; cje:Cj0317; -.
DR PATRIC; fig|192222.6.peg.309; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_7; -.
DR OMA; YPDMACT; -.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; Q9PII2; -.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..364
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153340"
FT MOD_RES 226
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:3GET"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:3GET"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3GET"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 272..295
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:3GET"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:3GET"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:3GET"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:3GET"
SQ SEQUENCE 364 AA; 41368 MW; E1CF525EB38804BC CRC64;
MKFNEFLNNL SNYEPGKDIE VIAKEYGVKE VIKLASNENP FGTPPKAIEC LRQNANKAHL
YPDDSMIELK STLAQKYKVQ NENIIIGAGS DQVIEFAIHS KLNSKNAFLQ AGVTFAMYEI
YAKQCGAKCY KTQSITHNLD EFKKLYETHK DEIKLIFLCL PNNPLGECLD ASEATEFIKG
VNEDCLVVID AAYNEFASFK DSKKHLEPCE LIKEFDNVLY LGTFSKLYGL GGLRIGYGIA
NANIISAFYK LRAPFNVSNL ALKAAVAAMD DDEFTEKTLE NNFSQMELYK EFAKKHNIKI
IDSYTNFITY FFDEKNSTDL SEKLLKKGII IRNLKSYGLN AIRITIGTSY ENEKFFTEFD
KILR
