HIS2_SALTY
ID HIS2_SALTY Reviewed; 203 AA.
AC P10367;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE Short=PRA-CH;
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE Short=PRA-PH;
DE EC=3.6.1.31;
GN Name=hisI; Synonyms=hisIE; OrderedLocusNames=STM2078;
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;
RX PubMed=3018428; DOI=10.1007/bf00422061;
RA Chiariotti L., Alifano P., Carlomagno M.S., Bruni C.B.;
RT "Nucleotide sequence of the Escherichia coli hisD gene and of the
RT Escherichia coli and Salmonella typhimurium hisIE region.";
RL Mol. Gen. Genet. 203:382-388(1986).
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=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000305}.
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DR EMBL; X13464; CAA31829.1; -; Genomic_DNA.
DR EMBL; X03975; CAA27614.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20982.1; -; Genomic_DNA.
DR PIR; B26022; YNEBHI.
DR RefSeq; NP_461023.1; NC_003197.2.
DR RefSeq; WP_000954848.1; NC_003197.2.
DR AlphaFoldDB; P10367; -.
DR SMR; P10367; -.
DR STRING; 99287.STM2078; -.
DR PaxDb; P10367; -.
DR EnsemblBacteria; AAL20982; AAL20982; STM2078.
DR GeneID; 1253599; -.
DR KEGG; stm:STM2078; -.
DR PATRIC; fig|99287.12.peg.2200; -.
DR HOGENOM; CLU_048577_3_1_6; -.
DR OMA; ERSCFHQ; -.
DR PhylomeDB; P10367; -.
DR BioCyc; SENT99287:STM2078-MON; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR Gene3D; 3.10.20.810; -; 1.
DR HAMAP; MF_01020; HisE; 1.
DR HAMAP; MF_01019; HisIE; 1.
DR InterPro; IPR023019; His_synth_HisIE.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF141734; SSF141734; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT CHAIN 1..203
FT /note="Histidine biosynthesis bifunctional protein HisIE"
FT /id="PRO_0000136427"
FT REGION 1..114
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 115..203
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT CONFLICT 70
FT /note="H -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="N -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22675 MW; 5B94D8D464C807EA CRC64;
MLTEQQRREL DWEKTDGLMP AIVQHAVSGE VLMLGYMNPQ ALDKTIESGH VTFFSRTKQR
LWTKGETSGH VLNVVSIAPD CDNDTLLVLA NPVGPTCHKG TSSCFGDASH QWLFLYQLEQ
LLAERKTADP TSSYTAKLYA SGTKRIAQKV GEEGVETALA ATVNDRFELT NEASDLMYHL
LVLLQDQDLN LTTVIDNLRK RHQ
