ID A0A317SLG8_9PEZI Unreviewed; 329 AA.
AC A0A317SLG8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000256|RuleBase:RU362021};
DE EC=2.7.7.1 {ECO:0000256|RuleBase:RU362021};
DE EC=2.7.7.18 {ECO:0000256|RuleBase:RU362021};
GN ORFNames=C7212DRAFT_281902 {ECO:0000313|EMBL:PWW75173.1};
OS Tuber magnatum (white Piedmont truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW75173.1, ECO:0000313|Proteomes:UP000246991};
RN [1] {ECO:0000313|EMBL:PWW75173.1, ECO:0000313|Proteomes:UP000246991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=091103-1 {ECO:0000313|EMBL:PWW75173.1};
RA Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362021};
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|ARBA:ARBA00001084,
CC ECO:0000256|RuleBase:RU362021};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004658, ECO:0000256|RuleBase:RU362021}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005019}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007064, ECO:0000256|RuleBase:RU362021}.
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:PWW75173.1}.
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DR EMBL; PYWC01000050; PWW75173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317SLG8; -.
DR STRING; 42249.A0A317SLG8; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000246991; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd09286; NMNAT_Eukarya; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1.
DR PANTHER; PTHR12039; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR12039:SF0; NICOTINAMIDE_NICOTINIC ACID MONONUCLEOTIDE ADENYLYLTRANSFERASE 1; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362021};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362021};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362021};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU362021};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU362021};
KW Reference proteome {ECO:0000313|Proteomes:UP000246991};
KW Transferase {ECO:0000256|RuleBase:RU362021, ECO:0000313|EMBL:PWW75173.1}.
FT DOMAIN 37..249
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 329 AA; 36714 MW; D49A296F5132FBB1 CRC64;
MVASSVSTPS PSFSEYTFPS HRLRALQDGT KTPLVLVACG SFSPITHMHL RMFEMAVDHV
KQGMSEFEVV GGYLSPVSDR YNKAGLASAA HRVRMCELAC DETSDWLMVD PWEAGQPEYQ
PTAVVLDHIS YEINHNLGGI PYPPPPLQST DYLTVPTTTT PRKPARLMLL GGSDLLQTMS
QPGVWSQSDL NHILTTHGLF IIERSGSDIS DALAPLKEWS DAAGKNWMEN IQFVRQLIAN
DISSTRIRQF LRQGMSVQYL LPQVVIEYIR ERGLYRDVEE FRENRASSMP PFTREAVDHA
VGKRRFVVAE GGEGCGDKEG EEAMRGRKV
//
