HIS22_BRADU
ID HIS22_BRADU Reviewed; 134 AA.
AC Q938W0;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase 2;
DE Short=PRA-PH 2;
DE EC=3.6.1.31;
GN Name=hisE2; Synonyms=his2; OrderedLocusNames=blr1323;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RA Mueller P.;
RT "A TnKPK2 insertion in the B. japonicum aspA gene causes the formation of
RT inflated symbiosomes within infected soybean nodule cells.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000305}.
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DR EMBL; AY046315; AAL02318.2; -; Genomic_DNA.
DR EMBL; BA000040; BAC46588.1; -; Genomic_DNA.
DR RefSeq; NP_767963.1; NC_004463.1.
DR RefSeq; WP_011084141.1; NZ_CP011360.1.
DR AlphaFoldDB; Q938W0; -.
DR SMR; Q938W0; -.
DR STRING; 224911.27349574; -.
DR EnsemblBacteria; BAC46588; BAC46588; BAC46588.
DR GeneID; 64021192; -.
DR KEGG; bja:blr1323; -.
DR PATRIC; fig|224911.44.peg.739; -.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_123337_1_3_5; -.
DR InParanoid; Q938W0; -.
DR OMA; YECADLW; -.
DR PhylomeDB; Q938W0; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000002526; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..134
FT /note="Phosphoribosyl-ATP pyrophosphatase 2"
FT /id="PRO_0000136351"
SQ SEQUENCE 134 AA; 14894 MW; 5702192AE3F55077 CRC64;
MSDSLERLYL AVLAARDLDP ATSRTARLFQ RGPSKMAKKL AEEAIEVVID AVNGDTDAVV
RESADLLYNL TVLWASAGVR PEDVWREMTR REDMLGIAEK LPKSAMKLPK VASPRVAARR
PIVALEGRTA RKRH
