ID Q3SPB4_NITWN Unreviewed; 221 AA.
AC Q3SPB4;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:ABA05877.1};
GN OrderedLocusNames=Nwi_2624 {ECO:0000313|EMBL:ABA05877.1};
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA05877.1, ECO:0000313|Proteomes:UP000002531};
RN [1] {ECO:0000313|EMBL:ABA05877.1, ECO:0000313|Proteomes:UP000002531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC {ECO:0000313|Proteomes:UP000002531};
RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000256|ARBA:ARBA00006506}.
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DR EMBL; CP000115; ABA05877.1; -; Genomic_DNA.
DR RefSeq; WP_011315827.1; NC_007406.1.
DR AlphaFoldDB; Q3SPB4; -.
DR STRING; 323098.Nwi_2624; -.
DR KEGG; nwi:Nwi_2624; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_040940_5_1_5; -.
DR OrthoDB; 9802805at2; -.
DR Proteomes; UP000002531; Chromosome.
DR GO; GO:0010945; F:coenzyme A diphosphatase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.
DR CDD; cd03426; CoAse; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR000059; NUDIX_hydrolase_NudL_CS.
DR PANTHER; PTHR12992:SF11; MITOCHONDRIAL COENZYME A DIPHOSPHATASE NUDT8; 1.
DR PANTHER; PTHR12992; NUDIX HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS01293; NUDIX_COA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABA05877.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002531}.
FT DOMAIN 59..190
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 221 AA; 24570 MW; 5D7315F676CE6EE6 CRC64;
MVRTGAAATT IGAGEFFDRA RERLRFDIPP GLTDAGIVPL TGDDDNDAVL RTIALETPIR
PAAVLIPVIA REQPTVLLTQ RAAHLKEHAG QIAFPGGKID ATDASPIDAA LREAWEEVGL
TRDFVEPIGY LDLYGTSFGF RILPTLARVR PGFDLRINTN EVDHAFEVPL SFLMNPLNHK
LGRKQFRGRT RSFYEMPFAE RNIWGATAGI LRVLYERVYL K
//
