HIS8_SALTY
ID HIS8_SALTY Reviewed; 359 AA.
AC P10369;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histidinol-phosphate aminotransferase;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase;
GN Name=hisC; OrderedLocusNames=STM2073;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=3062174; DOI=10.1016/0022-2836(88)90194-5;
RA Carlomagno M.S., Chiariotti L., Alifano P., Nappo A.G., Bruni C.B.;
RT "Structure and function of the Salmonella typhimurium and Escherichia coli
RT K-12 histidine operons.";
RL J. Mol. Biol. 203:585-606(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Barnes W.M., Husson R.N., Whittier R.;
RL Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; X13464; CAA31824.1; -; Genomic_DNA.
DR EMBL; J01804; AAA88616.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20977.1; -; Genomic_DNA.
DR PIR; JS0158; XNEBHC.
DR RefSeq; NP_461018.1; NC_003197.2.
DR RefSeq; WP_000102713.1; NC_003197.2.
DR AlphaFoldDB; P10369; -.
DR SMR; P10369; -.
DR STRING; 99287.STM2073; -.
DR PaxDb; P10369; -.
DR EnsemblBacteria; AAL20977; AAL20977; STM2073.
DR GeneID; 1253594; -.
DR KEGG; stm:STM2073; -.
DR PATRIC; fig|99287.12.peg.2195; -.
DR HOGENOM; CLU_017584_3_1_6; -.
DR OMA; IWLNANE; -.
DR PhylomeDB; P10369; -.
DR BioCyc; SENT99287:STM2073-MON; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001014; 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; 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; Reference proteome; Transferase.
FT CHAIN 1..359
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153444"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 148..164
FT /note="DGTKVVFVCSPNNPTGQ -> TAQKWCSFVAPIILPDN (in Ref. 2;
FT AAA88616)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="C -> R (in Ref. 1; CAA31824)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="L -> S (in Ref. 1; CAA31824)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..265
FT /note="GI -> ES (in Ref. 1; CAA31824)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="R -> P (in Ref. 1; CAA31824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39715 MW; 6241506A59CBB2A7 CRC64;
MSTENTLSVA DLARENVRNL VPYQSARRLG GNGDVWLNAN EFPTAVEFQL TQQTLNRYPE
CQPKAVIENY AQYAGVKPEQ VLVSRGADEG IELVIRAFCE PGKDAILYCP PTYGMYSVSA
ETIGVERRTV PALENWQLDL QGISDNLDGT KVVFVCSPNN PTGQLINPQD LRTLLELTRG
KAIVVADEAY IEFCPQATLT GWLVEYPHLV ILRTLSKAFA LAGLRCGFTL ANEEVINLLL
KVIAPYPLST PVADIAAQAL CPQGINAMRD RVAQTVQERQ YLVNALQQTA CVEHVFDSET
NYILARFTAS SSVFKSLWDQ GIILRDQNKQ PSLSGCLRIT VGTRQENQRV IDALRAEPV
