NADM_THEAC
ID NADM_THEAC Reviewed; 179 AA.
AC Q9HK34;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 97.
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=Ta0774;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11905.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445065; CAC11905.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048162318.1; NC_002578.1.
DR AlphaFoldDB; Q9HK34; -.
DR SMR; Q9HK34; -.
DR STRING; 273075.Ta0774; -.
DR EnsemblBacteria; CAC11905; CAC11905; CAC11905.
DR GeneID; 1456328; -.
DR KEGG; tac:Ta0774; -.
DR eggNOG; arCOG00972; Archaea.
DR HOGENOM; CLU_108783_0_0_2; -.
DR OMA; NSVWVSH; -.
DR OrthoDB; 90722at2157; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000001024; 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..179
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_0000135007"
SQ SEQUENCE 179 AA; 20934 MW; 80AE682D57A083A1 CRC64;
MESRKEKRAF LIGRFQPFHK GHLEIVKRIL SENDSIIIGI GSAQYSHTVV NPFTAGERHL
MISRTLEKER IYNYYLVPIE DVNANSLWVS HVEALTPKFD IVYTNNPLVR RLFMERKYEV
RSLPMVNRKE WTGTKIREKM IAGEPWENDV PDPVVEVIHE IDGISRIRQL STTDEDITQ
