ID   HIS2_PYRFU              Reviewed;         209 AA.
AC   P58853;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 106.
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=PF1664;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL81788.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009950; AAL81788.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014835587.1; NZ_CP023154.1.
DR   AlphaFoldDB; P58853; -.
DR   SMR; P58853; -.
DR   STRING; 186497.PF1664; -.
DR   DNASU; 1469541; -.
DR   EnsemblBacteria; AAL81788; AAL81788; PF1664.
DR   GeneID; 41713492; -.
DR   KEGG; pfu:PF1664; -.
DR   PATRIC; fig|186497.12.peg.1730; -.
DR   eggNOG; arCOG02676; Archaea.
DR   HOGENOM; CLU_048577_3_1_2; -.
DR   OMA; ERSCFHQ; -.
DR   OrthoDB; 77515at2157; -.
DR   PhylomeDB; P58853; -.
DR   UniPathway; UPA00031; UER00007.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000001013; 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_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; Reference proteome.
FT   CHAIN           1..209
FT                   /note="Histidine biosynthesis bifunctional protein HisIE"
FT                   /id="PRO_0000136455"
FT   REGION          1..123
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT   REGION          124..209
FT                   /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ   SEQUENCE   209 AA;  24236 MW;  E7F1BF99CCF2C5E8 CRC64;
     MEIEKLLEQV NWEKNNGIVP VIVQDEKGEV LTLAYMNKEA LRKTLETGIA HYYSRSKGRI
     RMKGEVSGNI QTVKEIKIDC DNDALLLIVS PKGPACHTGN YSCFYRKLGE PERVLPIDYS
     LSILKELEEI IKRRKETPVE GSYTSKLFKE GREKIYKKFG EEAIEVLVAE KRERIIYEVA
     DLLYHLLVLL TYNDISLGEV MNELRRRRK