ID A0A1F7QNG2_9BACT Unreviewed; 170 AA.
AC A0A1F7QNG2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=nicotinate-nucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012389};
DE EC=2.7.7.18 {ECO:0000256|ARBA:ARBA00012389};
GN ORFNames=A3F37_00900 {ECO:0000313|EMBL:OGL30418.1};
OS Candidatus Saccharibacteria bacterium RIFCSPHIGHO2_12_FULL_41_12.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1802138 {ECO:0000313|EMBL:OGL30418.1, ECO:0000313|Proteomes:UP000177946};
RN [1] {ECO:0000313|EMBL:OGL30418.1, ECO:0000313|Proteomes:UP000177946}
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 -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000256|ARBA:ARBA00002324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58437; EC=2.7.7.18;
CC Evidence={ECO:0000256|ARBA:ARBA00001785};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005019}.
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:OGL30418.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGCQ01000009; OGL30418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7QNG2; -.
DR STRING; 1802138.A3F37_00900; -.
DR Proteomes; UP000177946; Unassembled WGS sequence.
DR GO; GO:0070566; F:adenylyltransferase activity; IEA:UniProt.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR39321; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR39321:SF3; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}.
FT DOMAIN 6..167
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 170 AA; 19262 MW; E7D80A111A18F8BA CRC64;
MSAIGIFTGA FDPIHSGHLA FAHKALNLSL DKIYFLPEPK PRMKPNVSDL DDRISKLNKA
TEQDSRLGVI KLKQNNFEVQ SVLSELNQIF PDSKFVFLFG DDVLDHLANW KDLDIFAKET
EFLIATRNNS IGQISNVFKD FKLQGLGFNY QIIELNEGIS STEIRSRDTN
//