HIS2_ECOLI
ID HIS2_ECOLI Reviewed; 203 AA.
AC P06989; P78079; Q47596;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 171.
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=b2026, JW2008;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
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].
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 [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12;
RX PubMed=8201624; DOI=10.1006/jmbi.1994.1384;
RA Jovanovic G., Kostic T., Jankovic M., Savic D.J.;
RT "Nucleotide sequence of the Escherichia coli K12 histidine operon
RT revisited.";
RL J. Mol. Biol. 239:433-435(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O9:K31-:H- / F719;
RX PubMed=7536735; DOI=10.1128/jb.177.8.2178-2187.1995;
RA Kido N., Torgov V.I., Sugiyama T., Uchiya K., Sugihara H., Komatsu T.,
RA Kato N., Jann K.;
RT "Expression of the O9 polysaccharide of Escherichia coli: sequencing of the
RT E. coli O9 rfb gene cluster, characterization of mannosyl transferases, and
RT evidence for an ATP-binding cassette transport system.";
RL J. Bacteriol. 177:2178-2187(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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; X13462; CAA31818.1; -; Genomic_DNA.
DR EMBL; X03974; CAA27613.1; -; Genomic_DNA.
DR EMBL; U02072; AAA19744.1; -; Unassigned_DNA.
DR EMBL; D43637; BAA07753.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75087.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15858.1; -; Genomic_DNA.
DR PIR; JS0135; YNECHI.
DR RefSeq; NP_416530.1; NC_000913.3.
DR RefSeq; WP_000954911.1; NZ_SSUR01000003.1.
DR AlphaFoldDB; P06989; -.
DR SMR; P06989; -.
DR BioGRID; 4260421; 19.
DR DIP; DIP-9907N; -.
DR IntAct; P06989; 15.
DR STRING; 511145.b2026; -.
DR jPOST; P06989; -.
DR PaxDb; P06989; -.
DR PRIDE; P06989; -.
DR EnsemblBacteria; AAC75087; AAC75087; b2026.
DR EnsemblBacteria; BAA15858; BAA15858; BAA15858.
DR GeneID; 58390420; -.
DR GeneID; 946515; -.
DR KEGG; ecj:JW2008; -.
DR KEGG; eco:b2026; -.
DR PATRIC; fig|1411691.4.peg.226; -.
DR EchoBASE; EB0446; -.
DR eggNOG; COG0139; Bacteria.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_048577_3_1_6; -.
DR InParanoid; P06989; -.
DR OMA; ERSCFHQ; -.
DR PhylomeDB; P06989; -.
DR BioCyc; EcoCyc:HISTCYCLOPRATPPHOS; -.
DR BioCyc; MetaCyc:HISTCYCLOPRATPPHOS; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR PRO; PR:P06989; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; ISS:EcoCyc.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:EcoCyc.
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_0000136411"
FT REGION 1..114
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 115..203
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT VARIANT 5
FT /note="Q -> L (in strain: F719)"
FT VARIANT 46
FT /note="L -> I (in strain: F719)"
FT VARIANT 164
FT /note="H -> N (in strain: F719)"
FT VARIANT 192..193
FT /note="TT -> GE (in strain: F719)"
FT VARIANT 196
FT /note="E -> D (in strain: F719)"
FT VARIANT 199..200
FT /note="RK -> KN (in strain: F719)"
FT VARIANT 203
FT /note="Missing (in strain: F719)"
FT CONFLICT 68
FT /note="S -> P (in Ref. 1; CAA31818)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="T -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22756 MW; 34019009D82E0122 CRC64;
MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTLESGK VTFFSRTKQR
LWTKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ
LLAERKSADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL
LVLLQDQGLD LTTVIENLRK RHQ
