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Database: UniProt
Entry: A0A1I7SAG5_BURXY
LinkDB: A0A1I7SAG5_BURXY
Original site: A0A1I7SAG5_BURXY 
ID   A0A1I7SAG5_BURXY        Unreviewed;       228 AA.
AC   A0A1I7SAG5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   10-APR-2019, entry version 9.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|RuleBase:RU362021};
DE            EC=2.7.7.1 {ECO:0000256|RuleBase:RU362021};
DE            EC=2.7.7.18 {ECO:0000256|RuleBase:RU362021};
DE   AltName: Full=Nicotinate-nucleotide adenylyltransferase {ECO:0000256|RuleBase:RU362021};
OS   Bursaphelenchus xylophilus (Pinewood nematode worm) (Aphelenchoides
OS   xylophilus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Aphelenchoidea; Aphelenchoididae;
OC   Bursaphelenchus.
OX   NCBI_TaxID=6326 {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_1001200.1};
RN   [1] {ECO:0000313|Proteomes:UP000095284, ECO:0000313|WBParaSite:BXY_1001200.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21909270; DOI=10.1371/journal.ppat.1002219;
RA   Kikuchi T., Cotton J.A., Dalzell J.J., Hasegawa K., Kanzaki N.,
RA   McVeigh P., Takanashi T., Tsai I.J., Assefa S.A., Cock P.J.,
RA   Otto T.D., Hunt M., Reid A.J., Sanchez-Flores A., Tsuchihara K.,
RA   Yokoi T., Larsson M.C., Miwa J., Maule A.G., Sahashi N., Jones J.T.,
RA   Berriman M.;
RT   "Genomic insights into the origin of parasitism in the emerging plant
RT   pathogen Bursaphelenchus xylophilus.";
RL   PLoS Pathog. 7:e1002219-e1002219(2011).
RN   [2] {ECO:0000313|WBParaSite:BXY_1001200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-
CC         NAD(+) + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58437; EC=2.7.7.18;
CC         Evidence={ECO:0000256|RuleBase:RU362021};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) =
CC         diphosphate + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57540; EC=2.7.7.1;
CC         Evidence={ECO:0000256|RuleBase:RU362021};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1.
CC       {ECO:0000256|RuleBase:RU362021}.
CC   -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
CC       family. {ECO:0000256|RuleBase:RU362021}.
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DR   STRING; 6326.BUX.s01141.99; -.
DR   WBParaSite; BXY_1001200.1; BXY_1001200.1; BXY_1001200.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000095284; Whole Genome Shotgun Assembly.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00482; TIGR00482; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362021};
KW   Complete proteome {ECO:0000313|Proteomes:UP000095284};
KW   NAD {ECO:0000256|RuleBase:RU362021};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362021};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU362021};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|RuleBase:RU362021};
KW   Transferase {ECO:0000256|RuleBase:RU362021}.
FT   DOMAIN       14    201       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   228 AA;  25885 MW;  49089860148A6219 CRC64;
     MIPTRWNGAK VALLACGSFN PPTFMHLRMF ERARDLLQQE YKCTVVEGII SPVGDRYGKS
     ELISSSHRLR MCELAVRSSE WIRADGWECS QTSWTRTRVV LEHHRSVLQA KHGTDIQLIL
     LCGEDFVDSF AVVLASGENL WKSEDLSHIF TQYGVVCLQR VGGDARKTLE GLAVPKEHVS
     NVIFVQDETF PNSLSSTRLR NAIRNGLSIR YCSVDEVVEY VKEFSLYK
//
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