NADM_THEKO
ID NADM_THEKO Reviewed; 188 AA.
AC Q5JEF8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=TK0067;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD84256.1; -; Genomic_DNA.
DR RefSeq; WP_011249022.1; NC_006624.1.
DR AlphaFoldDB; Q5JEF8; -.
DR SMR; Q5JEF8; -.
DR STRING; 69014.TK0067; -.
DR EnsemblBacteria; BAD84256; BAD84256; TK0067.
DR GeneID; 3234497; -.
DR KEGG; tko:TK0067; -.
DR PATRIC; fig|69014.16.peg.68; -.
DR eggNOG; arCOG00972; Archaea.
DR HOGENOM; CLU_108783_0_0_2; -.
DR InParanoid; Q5JEF8; -.
DR OMA; NSVWVSH; -.
DR OrthoDB; 90722at2157; -.
DR PhylomeDB; Q5JEF8; -.
DR BRENDA; 2.7.7.1; 5246.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000000536; 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; -; 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 Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR01527; arch_NMN_Atrans; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..188
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_0000135002"
SQ SEQUENCE 188 AA; 21699 MW; 64D6A3977160540C CRC64;
MVKRGLFVGR FQPVHNGHIK ALEFVFSQVD EVIIGIGSAQ ASHTLKNPFT TSERMEMLIR
ALEEAELTEK RYYLIPLPDI NFNAIWATYV VSMVPRFDVV FTGNSLVAQL FREKGYEVIV
QPMFRKDILS ATEIRRRMVE GEPWEELVPR SVAEFIREIK GVERIKMLAT NLESSEKELQ
APIRIPEF
