ID H0TNY6_9BRAD Unreviewed; 133 AA.
AC H0TNY6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01020};
DE Short=PRA-PH {ECO:0000256|HAMAP-Rule:MF_01020};
DE EC=3.6.1.31 {ECO:0000256|HAMAP-Rule:MF_01020};
GN Name=hisE {ECO:0000256|HAMAP-Rule:MF_01020};
GN ORFNames=BRAS3843_2630018 {ECO:0000313|EMBL:CCE08174.1};
OS Bradyrhizobium sp. STM 3843.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE08174.1, ECO:0000313|Proteomes:UP000002686};
RN [1] {ECO:0000313|Proteomes:UP000002686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX PubMed=24704842; DOI=10.3390/genes3010035;
RA Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA Smith A.A., Giraud E., Medigue C., Moulin L.;
RT "Comparative genomics of aeschynomene symbionts: insights into the
RT ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL Genes (Basel) 3:35-61(2011).
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:0000256|ARBA:ARBA00001460, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00005204, ECO:0000256|HAMAP-Rule:MF_01020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01020}.
CC -!- SIMILARITY: Belongs to the PRA-PH family.
CC {ECO:0000256|ARBA:ARBA00009392, ECO:0000256|HAMAP-Rule:MF_01020}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCE08174.1}.
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DR EMBL; CAFK01000183; CCE08174.1; -; Genomic_DNA.
DR RefSeq; WP_008970686.1; NZ_CAFK01000183.1.
DR AlphaFoldDB; H0TNY6; -.
DR OrthoDB; 9814738at2; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000002686; Unassembled WGS sequence.
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 Gene3D; 1.10.287.1080; MazG-like; 1.
DR HAMAP; MF_01020; HisE; 1.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR NCBIfam; TIGR03188; histidine_hisI; 1.
DR PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01020};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01020}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01020};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01020};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01020};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01020}; Reference proteome {ECO:0000313|Proteomes:UP000002686}.
SQ SEQUENCE 133 AA; 14882 MW; 5558DE7A568594B1 CRC64;
MSDSIERLYL AVLAARDQDP GRSRTAKLLQ QGTAKMAKKL TEEAIEVAID AVRGDAQSVV
RESADLIYNL AVLWAETGVR PDDVWREMER REVLLGIAEK LPKSPVKIQK SANARLARRP
IVALEGRALR KRH
//