ID A0A0D5A9Q2_9NOCA Unreviewed; 311 AA.
AC A0A0D5A9Q2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydrolase MutT1 {ECO:0000313|EMBL:AJW39518.1};
GN ORFNames=NY08_1488 {ECO:0000313|EMBL:AJW39518.1};
OS Rhodococcus sp. B7740.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW39518.1, ECO:0000313|Proteomes:UP000032410};
RN [1] {ECO:0000313|EMBL:AJW39518.1, ECO:0000313|Proteomes:UP000032410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7740 {ECO:0000313|EMBL:AJW39518.1};
RX PubMed=25931596;
RA Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT Bacterium Isolated from the Arctic Sea.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005582, ECO:0000256|RuleBase:RU003476}.
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DR EMBL; CP010797; AJW39518.1; -; Genomic_DNA.
DR RefSeq; WP_032397769.1; NZ_CP010797.1.
DR AlphaFoldDB; A0A0D5A9Q2; -.
DR STRING; 1564114.NY08_1488; -.
DR KEGG; rhb:NY08_1488; -.
DR PATRIC; fig|1564114.4.peg.1459; -.
DR HOGENOM; CLU_048989_0_0_11; -.
DR Proteomes; UP000032410; 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; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR PANTHER; PTHR21340:SF8; NUDIX HYDROLASE; 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}.
FT DOMAIN 10..141
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 311 AA; 34216 MW; 850D34BD8AE03C88 CRC64;
MGTSDGSPRA NIFAAGSILW RRSPSGDSGV EVALVHRPKY DDWSFPKGKL DPGETAVDAA
VREVKEETGF DSRLGRSLSY VTYPIPGHRR VKKVLYWAAE VTGGEFVPNV EVDELRWVAP
EDVGRELSYP MDHKILRRFV AKPADTSTVL LVRHGSAGSR SRFKGNDVDR PLDRTGRRQA
QSLVSLLRAF GGDSVYAADR ARCVQTVAPF AESLGVDITP EHLLSEEGYA DDPRKGRHRA
RDIAELPGTP VVCSQGKVIP DLMRWWAEKD GITLPANRNR KGSVWVLSRR DGRLIAADHI
ASPLPTLTAD G
//
