ID C3NFV0_SULIN Unreviewed; 142 AA.
AC C3NFV0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00243};
DE EC=2.7.7.1 {ECO:0000256|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00243};
DE AltName: Full=NMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00243};
GN OrderedLocusNames=YN1551_0959 {ECO:0000313|EMBL:ACP48068.1};
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942 {ECO:0000313|EMBL:ACP48068.1, ECO:0000313|Proteomes:UP000006818};
RN [1] {ECO:0000313|EMBL:ACP48068.1, ECO:0000313|Proteomes:UP000006818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2 {ECO:0000313|Proteomes:UP000006818};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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:0000256|HAMAP-Rule:MF_00243};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00243}.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010124, ECO:0000256|HAMAP-Rule:MF_00243}.
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DR EMBL; CP001404; ACP48068.1; -; Genomic_DNA.
DR AlphaFoldDB; C3NFV0; -.
DR KEGG; sin:YN1551_0959; -.
DR HOGENOM; CLU_108783_0_0_2; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000006818; 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 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 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 {ECO:0000256|HAMAP-Rule:MF_00243};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00243};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00243};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00243};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00243};
KW Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00243};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00243}.
FT DOMAIN 2..105
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 142 AA; 16569 MW; 00686B1937E213BA CRC64;
MIILVGSSQE SHTVTNPFTA GERVEMIRNS LKYSGIDLSR IFIIPMPDIL MNNIWAHYVS
TYTPKFEVVF ARNPLVVRIF KEAGYKVEIP PAFNREKYNS TYIRRLIILN DNWSELVPEP
VYKYILHIHG DQRLREIVGT DK
//
