ID A0A1E5PIP9_9ACTN Unreviewed; 302 AA.
AC A0A1E5PIP9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=AS594_12180 {ECO:0000313|EMBL:OEJ29396.1};
OS Streptomyces agglomeratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ29396.1, ECO:0000313|Proteomes:UP000095759};
RN [1] {ECO:0000313|EMBL:OEJ29396.1, ECO:0000313|Proteomes:UP000095759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ29396.1,
RC ECO:0000313|Proteomes:UP000095759};
RA Chen X.;
RT "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OEJ29396.1}.
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DR EMBL; MEHJ01000001; OEJ29396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5PIP9; -.
DR STRING; 285458.BGM19_24630; -.
DR OrthoDB; 9791656at2; -.
DR Proteomes; UP000095759; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd03429; NADH_pyrophosphatase; 1.
DR Gene3D; 3.90.79.20; -; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR049734; NudC-like_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015376; Znr_NADH_PPase.
DR PANTHER; PTHR11383:SF3; NAD(P)H PYROPHOSPHATASE NUDT13, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11383; NUCLEOSIDE DIPHOSPHATE-LINKED MOIETY X MOTIF 13; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR Pfam; PF09297; zf-NADH-PPase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000095759}.
FT DOMAIN 159..283
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 302 AA; 33126 MW; 3CC8774503701CCA CRC64;
MGLTAPSGID RAAHHRLDEA WLAAAWSHPT TRVFVVSGGQ ALIDDTPDGR TELVMTPAFE
APVTETHRYF LGTDEDGVSY FALQKDSLPG RMDQSARPAG LREAGLLLGP RDAGLMVHAV
ALENWQRLHR FCSRCGERTV IAAAGHIRRC QACGAEHYPR TDPAVIMLVT DEEDRALLGR
QVHWPEGRFS TLAGFVEPGE TIEESVAREV FEEAGVTVGR VEYVASQPWP FPSSLMLGFM
ARATSSEINV DGDEIEEARW FSRDDLRAAI ESGEILPPSG ISIAARLVEL WYGEPLPKPV
NP
//
