HIS2_BACCR
ID HIS2_BACCR Reviewed; 107 AA.
AC Q81G00;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01020};
DE Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01020};
DE EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01020};
GN Name=hisE {ECO:0000255|HAMAP-Rule:MF_01020}; OrderedLocusNames=BC_1412;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01020};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000255|HAMAP-Rule:MF_01020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01020}.
CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000255|HAMAP-
CC Rule:MF_01020}.
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DR EMBL; AE016877; AAP08393.1; -; Genomic_DNA.
DR RefSeq; NP_831192.1; NC_004722.1.
DR RefSeq; WP_000426358.1; NZ_CP034551.1.
DR PDB; 1YVW; X-ray; 2.60 A; A/B/C/D=1-107.
DR PDBsum; 1YVW; -.
DR AlphaFoldDB; Q81G00; -.
DR SMR; Q81G00; -.
DR STRING; 226900.BC_1412; -.
DR EnsemblBacteria; AAP08393; AAP08393; BC_1412.
DR GeneID; 67506115; -.
DR KEGG; bce:BC1412; -.
DR PATRIC; fig|226900.8.peg.1389; -.
DR HOGENOM; CLU_123337_0_0_9; -.
DR OMA; FTHEKGE; -.
DR UniPathway; UPA00031; UER00007.
DR EvolutionaryTrace; Q81G00; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 HAMAP; MF_01020; HisE; 1.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR Pfam; PF01503; PRA-PH; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Histidine biosynthesis; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..107
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000136345"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:1YVW"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:1YVW"
FT HELIX 33..52
FT /evidence="ECO:0007829|PDB:1YVW"
FT HELIX 56..76
FT /evidence="ECO:0007829|PDB:1YVW"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:1YVW"
SQ SEQUENCE 107 AA; 12446 MW; A2B1899D636C7316 CRC64;
MENAFKLLYK TIEERKGSPL PESYTNYLFS KGEDKILKKI GEECAEVIIA CKNNDKEEVV
KEMVDVFYHC FVLLAEKNIA LEDVMREVKE RNGKLSRVGD RREIDTL
