ID I0YK30_COCSC Unreviewed; 551 AA.
AC I0YK30;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=NAD(+) diphosphatase {ECO:0000256|ARBA:ARBA00012381};
DE EC=3.6.1.22 {ECO:0000256|ARBA:ARBA00012381};
GN ORFNames=COCSUDRAFT_49188 {ECO:0000313|EMBL:EIE18749.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE18749.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE18749.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE18749.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC ChEBI:CHEBI:144051; Evidence={ECO:0000256|ARBA:ARBA00023679};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC Evidence={ECO:0000256|ARBA:ARBA00023679};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC {ECO:0000256|ARBA:ARBA00009595}.
CC -!- SIMILARITY: Belongs to the janus family.
CC {ECO:0000256|ARBA:ARBA00010971}.
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:EIE18749.1}.
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DR EMBL; AGSI01000022; EIE18749.1; -; Genomic_DNA.
DR RefSeq; XP_005643293.1; XM_005643236.1.
DR AlphaFoldDB; I0YK30; -.
DR STRING; 574566.I0YK30; -.
DR GeneID; 17036678; -.
DR KEGG; csl:COCSUDRAFT_49188; -.
DR eggNOG; KOG3084; Eukaryota.
DR OrthoDB; 3024612at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
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; 3.50.20.20; Janus/Ocnus; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007702; Janus.
DR InterPro; IPR038596; Janus_sf.
DR InterPro; IPR015375; NADH_PPase-like_N.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR42904:SF8; NAD(+) DIPHOSPHATASE; 1.
DR PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR Pfam; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR Pfam; PF05005; Ocnus; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR SUPFAM; SSF143724; PHP14-like; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
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:UP000007264}.
FT DOMAIN 216..380
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT ACT_SITE 479
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR607702-1"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR607702-2"
SQ SEQUENCE 551 AA; 60200 MW; 898F191F3ED3FF38 CRC64;
MSDMLLRFGQ FARSTRLYIG SGSLRGTHVG CRIATSARLE RINDGDAAAL HYAGLGLDRA
THIRNDEAKL KELAGRSDAK LVPVFEGKNL VTHSQGLSSA VLPLQNAEQY LIPDSLVFLG
LEPGGVPVFG AACRPECEEW LSPLVAEAGA GARWVDLRKE GPKLAGDQAA LLALAQALLR
WNENNAFCGR TGAPTAAMQG GHARVAASPR ARVVYPRIDP AVIALVYCGD YALLGRQSRW
APGRYSCLAG FAEVGETLEL AVGREVKEES GVAVDPHSIQ YVASQPWPFP QSLMIGFMAT
AAAPDRSHAW SLARQRLQGL HHGCTEEEVG FTLVEELCLQ QPLVDITELE DARWFHRSWL
RRHLHHAADG SGWDTSEAES SSSTAASVSF SIPGSYALAH RLIHTFMALE QPAKGDARHW
RQARIQTCHC VMAFDAVPDV KEVDIDESGT YKYVLLRLQS KSNSMSRLLV RGNKRAGYHQ
DILELAQEVD ADDDSQVVPL GGGRIAFDEE KRTIDIYGFS SAYDQAPHDI TAALVRRSYP
FHTVSVSYSG Y
//