ID   HIS2_THEP3              Reviewed;         216 AA.
AC   Q9RPQ3;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 81.
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;
OS   Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS   thermohydrosulfuricum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=340099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10594232; DOI=10.1007/s002849910029;
RA   Erbeznik M., Strobel H.J., Dawson K.A.;
RT   "Organization and sequence of histidine biosynthesis genes hisH, -A, -F,
RT   and -IE in Thermoanaerobacter ethanolicus.";
RL   Curr. Microbiol. 40:140-142(2000).
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 {ECO:0000250}.
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; AF150930; AAF05095.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RPQ3; -.
DR   SMR; Q9RPQ3; -.
DR   UniPathway; UPA00031; UER00007.
DR   UniPathway; UPA00031; UER00008.
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_01021; HisI; 1.
DR   HAMAP; MF_01019; HisIE; 1.
DR   InterPro; IPR023019; His_synth_HisIE.
DR   InterPro; IPR008179; HisE.
DR   InterPro; IPR026660; PRA-CH.
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..216
FT                   /note="Histidine biosynthesis bifunctional protein HisIE"
FT                   /id="PRO_0000136441"
FT   REGION          1..132
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT   REGION          133..216
FT                   /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ   SEQUENCE   216 AA;  25005 MW;  1230E351B36C35D5 CRC64;
     MENILKELKF DDRGLIPVIT QDYKTNEVLM MAYIMKRPLK KSLETGKVHY FSRSRNKLWL
     KGETSGHFQL IKSISIDCDA DTLLIKVEQV EAACHTGHYS CFYREISGNE LKETSDKVFD
     EQKVYEAENA KILQEIYDVI VDRTIHPKEG SYTNYLFEKG LDKILKKVGE EAAEVIIGAK
     NRDKGEIVYE ISDLIYHLLV LMVERGIKLE DIYEEA