ID A0A1F7W9R7_9BACT Unreviewed; 168 AA.
AC A0A1F7W9R7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
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 ORFNames=A2304_05510 {ECO:0000313|EMBL:OGL99561.1};
OS Candidatus Uhrbacteria bacterium RIFOXYB2_FULL_57_15.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802422 {ECO:0000313|EMBL:OGL99561.1, ECO:0000313|Proteomes:UP000176501};
RN [1] {ECO:0000313|EMBL:OGL99561.1, ECO:0000313|Proteomes:UP000176501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGL99561.1}.
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DR EMBL; MGFE01000002; OGL99561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7W9R7; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000176501; Unassembled WGS sequence.
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; 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 {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|HAMAP-Rule:MF_00243}.
FT DOMAIN 7..137
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 168 AA; 18749 MW; 108BF5D82A59A39B CRC64;
MSAFSCLFVG RFQPFHNGHL MVIKGMTKVC GKIVVAIGSP EAEKGIENPF TAAERREMIQ
RALQGVDIIP NFDISIIEVP DVGDDETWAK KCLELSEEVH QVWTGNEWTK SCFEKVGLEV
KDIKEVPGIS ATEIRKRMKE GGDWRALVPG EVASYLSELN ASERIKNL
//
