ID   HIS2_LACLA              Reviewed;         212 AA.
AC   Q02130; Q9CG90;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-MAY-2022, entry version 127.
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=LL1215; ORFNames=L0072;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCDO 2118;
RX   PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA   Delorme C., Ehrlich S.D., Renault P.;
RT   "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL   J. Bacteriol. 174:6571-6579(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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 {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; U92974; AAB81910.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK05313.1; -; Genomic_DNA.
DR   PIR; C47754; C47754.
DR   PIR; G86776; G86776.
DR   RefSeq; NP_267371.1; NC_002662.1.
DR   RefSeq; WP_003131119.1; NC_002662.1.
DR   AlphaFoldDB; Q02130; -.
DR   SMR; Q02130; -.
DR   STRING; 272623.L0072; -.
DR   PaxDb; Q02130; -.
DR   EnsemblBacteria; AAK05313; AAK05313; L0072.
DR   KEGG; lla:L0072; -.
DR   PATRIC; fig|272623.7.peg.1312; -.
DR   eggNOG; COG0139; Bacteria.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_048577_3_1_9; -.
DR   OMA; ERSCFHQ; -.
DR   UniPathway; UPA00031; UER00007.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000002196; 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..212
FT                   /note="Histidine biosynthesis bifunctional protein HisIE"
FT                   /id="PRO_0000136418"
FT   REGION          1..109
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT   REGION          110..212
FT                   /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT   CONFLICT        93
FT                   /note="T -> A (in Ref. 1; AAB81910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="I -> T (in Ref. 1; AAB81910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   212 AA;  24717 MW;  7686EB6B923323E1 CRC64;
     MRPDFHKQEL IPVIVQDYQT NQVLMLAYTN EVAFEKMLET GETWFWSRSR QKLWHKGEES
     GHFQKIKGMR LDCDQDTLLV FVEQIGNACH TGTYSCFYDE LIPFDDSDIF SELEKQIIDR
     KLHPVEKSYT NYLLGEGIDK VLKKVGEEAS EVIIASKNSD KGELLGEIDD LLYHLFVLMN
     QQGISLEEVR QKAKERHQLE GNKKEFHTRT AD