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Database: UniProt
Entry: A0A2S7Q4I6_9HELO
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ID   A0A2S7Q4I6_9HELO        Unreviewed;       289 AA.
AC   A0A2S7Q4I6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=CJF30_00008323 {ECO:0000313|EMBL:PQE21461.1};
OS   Rutstroemia sp. NJR-2017a BBW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Rutstroemiaceae; Rutstroemia.
OX   NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE21461.1, ECO:0000313|Proteomes:UP000238072};
RN   [1] {ECO:0000313|EMBL:PQE21461.1, ECO:0000313|Proteomes:UP000238072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE21461.1,
RC   ECO:0000313|Proteomes:UP000238072};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-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:PQE21461.1}.
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DR   EMBL; NJPT01000028; PQE21461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7Q4I6; -.
DR   STRING; 2070414.A0A2S7Q4I6; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000238072; 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:UP000238072};
KW   Transferase {ECO:0000256|RuleBase:RU362021, ECO:0000313|EMBL:PQE21461.1}.
FT   DOMAIN          41..227
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   REGION          258..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  31945 MW;  1538053035A4B30F CRC64;
     MASDPPAQTA PAAQTLENYT FPTNRLRLQQ NDPNKTPLVL VACGSFSPIT YLHLRMMEMA
     ADYCKFNTDF ELLSGYFSPV SNFYKKAGLA SSVHRINMCE LAVQSSSWLM VDPWEALQTE
     YTPTALVLDH VEHEINTVLG GAIRPDGSRV PVRIALLAGA DLIETMSIPG VWSEADLQHI
     LGQYGTFIVE RAGTDIEDAL ASLEQYKRNI YVIQQLVTND ISSTKIRLFL RKEMSVQYLL
     PAPVIEYIEE HHLYEEDGAS SIDTRGKAKA SEGSGRASPA VESSNQKGS
//
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