ID A0A1L8FKV8_XENLA Unreviewed; 319 AA.
AC A0A1L8FKV8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Name=nmnat1.L {ECO:0000313|RefSeq:XP_018079692.1,
GN ECO:0000313|RefSeq:XP_018079693.1,
GN ECO:0000313|Xenbase:XB-GENE-993373};
GN Synonyms=nmnat1 {ECO:0000313|RefSeq:XP_018079692.1,
GN ECO:0000313|RefSeq:XP_018079693.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018079692.1};
RN [1] {ECO:0000313|RefSeq:XP_018079692.1, ECO:0000313|RefSeq:XP_018079693.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018079692.1,
RC ECO:0000313|RefSeq:XP_018079693.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018079692.1,
RC ECO:0000313|RefSeq:XP_018079693.1};
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
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:ARBA00033662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22861;
CC Evidence={ECO:0000256|ARBA:ARBA00033662};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22862;
CC Evidence={ECO:0000256|ARBA:ARBA00033662};
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:ARBA00033693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21361;
CC Evidence={ECO:0000256|ARBA:ARBA00033693};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21362;
CC Evidence={ECO:0000256|ARBA:ARBA00033693};
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 RefSeq; XP_018079692.1; XM_018224203.2.
DR RefSeq; XP_018079693.1; XM_018224204.2.
DR STRING; 8355.A0A1L8FKV8; -.
DR PaxDb; 8355-A0A1L8FKV8; -.
DR GeneID; 100036953; -.
DR AGR; Xenbase:XB-GENE-993373; -.
DR CTD; 100036953; -.
DR Xenbase; XB-GENE-993373; nmnat1.L.
DR OMA; HFDYELN; -.
DR OrthoDB; 5488885at2759; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 100036953; Expressed in neurula embryo and 19 other cell types or tissues.
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:UniProtKB-EC.
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 ECO:0000313|RefSeq:XP_018079692.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU362021};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Transferase {ECO:0000256|RuleBase:RU362021}.
FT DOMAIN 54..268
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 159..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 319 AA; 36890 MW; 6920B2D25B15EF2F CRC64;
MRKIKQWGFC LNVWKFCRCT ISLSSRSHLA SSDAIYQPLQ NMEKSDDRTE VVLLATGSFN
PITVMHLRLF ELARDYLHDT GKYKVIKGII SPVCDGYKKK GLIEASHRLA MANLATKTSD
WLEVDSWECS QKQWTETVLV LRHHQQKLTN ANIVDTWEKD AHKKGHKRKR ENSHQDKPNS
YLQENKAVPQ VKLLCGADML ESLGKPNLWK NEDVIEILSS FGIICITRLG SNASNFIYES
DILWKYKHMI HLVEEWITND ISSTKIRRAL RRGMSIRYLV PDSVVEYIQN HELYSEESEE
KNSGVILEPL ARNTKDSQL
//
