ID NADM_THEON Reviewed; 187 AA.
AC B6YX39;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00243};
DE EC=2.7.7.1 {ECO:0000255|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00243};
DE AltName: Full=NMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00243};
GN OrderedLocusNames=TON_1164;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00243};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00243}.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00243}.
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DR EMBL; CP000855; ACJ16652.1; -; Genomic_DNA.
DR RefSeq; WP_012572124.1; NC_011529.1.
DR AlphaFoldDB; B6YX39; -.
DR SMR; B6YX39; -.
DR STRING; 523850.TON_1164; -.
DR GeneID; 7018186; -.
DR KEGG; ton:TON_1164; -.
DR PATRIC; fig|523850.10.peg.1171; -.
DR eggNOG; arCOG00972; Archaea.
DR HOGENOM; CLU_108783_0_0_2; -.
DR OrthoDB; 264480at2157; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02166; NMNAT_Archaea; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00243; NMN_adenylyltr; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR006418; NMN_Atrans_arc.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR01527; arch_NMN_Atrans; 1.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR21342:SF0; BIFUNCTIONAL NMN ADENYLYLTRANSFERASE_NUDIX HYDROLASE; 1.
DR PANTHER; PTHR21342; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Transferase.
FT CHAIN 1..187
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_1000100758"
SQ SEQUENCE 187 AA; 21526 MW; B4679FA82F9980EE CRC64;
MPKRGLFVGR FQPVHNGHIK ALEFVFSQVD EVIIGIGSAQ ASHTLKNPFT TSERMEMLIR
ALDEAGLEKR YYLIPLPDIN FNAIWSTYVQ SMVPRFDVVF TGNSLVAQLF RERGYEVIVQ
PMFRKDILSA TEIRKRMVEG EPWEELVPKS VAEFIKEIKG VERIKMLATN LENSEKELQA
PIRIPEF
//
