HIS2_SHISS
ID HIS2_SHISS Reviewed; 203 AA.
AC Q3Z0F9;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000250|UniProtKB:Q9S5G3};
DE Short=PRA-CH {ECO:0000250|UniProtKB:Q9S5G3};
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000250|UniProtKB:Q9S5G3};
DE Short=PRA-PH {ECO:0000250|UniProtKB:Q9S5G3};
DE EC=3.6.1.31;
GN Name=hisI {ECO:0000312|EMBL:AAZ88753.1}; Synonyms=hisIE;
GN OrderedLocusNames=SSON_2097;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1] {ECO:0000312|EMBL:AAZ88753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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 {ECO:0000250|UniProtKB:Q9S5G3}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000250|UniProtKB:Q9S5G3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9S5G3}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC {ECO:0000255}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000255}.
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DR EMBL; CP000038; AAZ88753.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z0F9; -.
DR SMR; Q3Z0F9; -.
DR EnsemblBacteria; AAZ88753; AAZ88753; SSON_2097.
DR KEGG; ssn:SSON_2097; -.
DR HOGENOM; CLU_048577_3_1_6; -.
DR OMA; ERSCFHQ; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000002529; 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.
FT CHAIN 1..203
FT /note="Histidine biosynthesis bifunctional protein HisIE"
FT /id="PRO_0000390789"
FT REGION 1..114
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000255"
FT REGION 115..203
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 203 AA; 22841 MW; 26F0100EDF4DD60D CRC64;
MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTIESGK VTFFSRTKQR
LWTKGETSGN FLNVVNIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ
LLAERKSADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL
LVLLQDQDLD LTTVIENLRK RHQ
