ID D2Q7R5_BIFDB Unreviewed; 358 AA.
AC D2Q7R5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Phosphohydrolase (MutT/NUDIX family protein) {ECO:0000313|EMBL:ADB08886.1};
GN OrderedLocusNames=BDP_0204 {ECO:0000313|EMBL:ADB08886.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB08886.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB08886.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU003476}.
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DR EMBL; CP001750; ADB08886.1; -; Genomic_DNA.
DR AlphaFoldDB; D2Q7R5; -.
DR STRING; 401473.BDP_0204; -.
DR KEGG; bde:BDP_0204; -.
DR eggNOG; COG0494; Bacteria.
DR eggNOG; COG2062; Bacteria.
DR HOGENOM; CLU_048989_1_0_11; -.
DR Proteomes; UP000008693; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03673; Ap6A_hydrolase; 1.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR21340:SF0; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [ASYMMETRICAL]; 1.
DR PANTHER; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003476};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT DOMAIN 12..175
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 358 AA; 40225 MW; 99534D7168BEB7CC CRC64;
MRRIVEAAGG IVYRWKVGGQ IADNPQIATR KTAKELLDDI EVCIVHRPKY DDWSWPKGKL
EQGESHRHAA VREIGEETGV SIALGPYLGE VEYPLSEEGK KTRHSHDRTV DTKHTLYWMA
RPITGEDAEH LIDAFGPVHR ADVGEINDIV WVSVREARKI LTHSTDKDIL AAFVDRVQEG
AATAQNLLIV RHAKAESRKS WKGTDANRPI TPKGAAAAFA LNRELACYNP TRLATSPWMR
CQETLQVLSW QTDRPMEHID ALTEDAFADH PTMAWLAFLD QIRQTLNTRQ TTAICMHRPV
IGGMFDHLRG MCSRKQLAKQ LIAKSPYMPT GTAIAMFIID TPQGPNIIDI QKVTPLVY
//
