ID A0A0D2IDY1_9EURO Unreviewed; 269 AA.
AC A0A0D2IDY1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=Z518_07557 {ECO:0000313|EMBL:KIX04004.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX04004.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX04004.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX04004.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847479; KIX04004.1; -; Genomic_DNA.
DR RefSeq; XP_013271140.1; XM_013415686.1.
DR AlphaFoldDB; A0A0D2IDY1; -.
DR STRING; 1442369.A0A0D2IDY1; -.
DR GeneID; 25295628; -.
DR VEuPathDB; FungiDB:Z518_07557; -.
DR HOGENOM; CLU_033366_0_1_1; -.
DR OrthoDB; 5488885at2759; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362021};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362021};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU362021,
KW ECO:0000313|EMBL:KIX04004.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU362021};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Transferase {ECO:0000256|RuleBase:RU362021, ECO:0000313|EMBL:KIX04004.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..213
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 30332 MW; D1EE1E310BD890E4 CRC64;
MDEYHFPDSR LKKKMDDPSK TPLLLVACGS FSPITFLHLR MFVMAADYVK HNTDFEMVGG
YLSPVSDAYK KQGLAPAEHR VAMCQLAIDR ASSWLMVDTW EAEKKEYQPT AKVLDHFDHE
INVIRKGIDT GDGNRKPVRI ALLAGADLIQ TMSTPGVWSE KDLDHILGRY GTFIIERSGT
DIDEALASLQ SYRDNIYVIQ QLIQNDVSST KIRLFLRRGM SVQYLIPAPV VEYIEQNHLY
EDDGRASSMT SITHADSDKG KAKEVQSTS
//
