HIS2_CERS4
ID HIS2_CERS4 Reviewed; 103 AA.
AC P50935; Q3J488;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE Short=PRA-PH;
DE EC=3.6.1.31;
GN Name=hisE; OrderedLocusNames=RHOS4_08280; ORFNames=RSP_2241;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8760919; DOI=10.1099/13500872-142-8-2071;
RA Oriol E., Mendez-Alvarez S., Barbe J., Gibert I.;
RT "Cloning of the Rhodobacter sphaeroides hisL gene: unifunctionality of the
RT encoded protein and lack of linkage to other his genes.";
RL Microbiology 142:2071-2078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; X87256; CAA60711.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA78396.1; -; Genomic_DNA.
DR PIR; S54839; S54839.
DR RefSeq; WP_011337341.1; NZ_CP030271.1.
DR RefSeq; YP_352297.1; NC_007493.2.
DR AlphaFoldDB; P50935; -.
DR SMR; P50935; -.
DR STRING; 272943.RSP_2241; -.
DR PRIDE; P50935; -.
DR EnsemblBacteria; ABA78396; ABA78396; RSP_2241.
DR KEGG; rsp:RSP_2241; -.
DR PATRIC; fig|272943.9.peg.1144; -.
DR eggNOG; COG0140; Bacteria.
DR OMA; FTHEKGE; -.
DR PhylomeDB; P50935; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000002703; Chromosome 1.
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..103
FT /note="Phosphoribosyl-ATP pyrophosphatase"
FT /id="PRO_0000136386"
FT CONFLICT 102
FT /note="R -> P (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 10900 MW; 912D942321EE45C8 CRC64;
MTVLERLAAT VEARKGADPD SSWTAKLFAK GPEKCAEKFG EEAVEAIIEA VRGDRAKLAS
EAADVLYHLL VMLAARDVTL AEVMAVLEAR EGTSGIAEKA GRG
