NMNA2_XENTR
ID NMNA2_XENTR Reviewed; 307 AA.
AC A4IH61;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000305};
DE Short=NMN/NaMN adenylyltransferase 2;
DE EC=2.7.7.1 {ECO:0000250|UniProtKB:Q9BZQ4};
DE EC=2.7.7.18 {ECO:0000250|UniProtKB:Q9BZQ4};
DE AltName: Full=Nicotinamide mononucleotide adenylyltransferase 2;
DE Short=NMN adenylyltransferase 2;
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 2;
DE Short=NaMN adenylyltransferase 2;
GN Name=nmnat2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
CC mononucleotide (NMN) and ATP. Can also use the deamidated form;
CC nicotinic acid mononucleotide (NaMN) as substrate (By similarity).
CC {ECO:0000250}.
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:0000250|UniProtKB:Q9BZQ4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21361;
CC Evidence={ECO:0000250|UniProtKB:Q9BZQ4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21362;
CC Evidence={ECO:0000250|UniProtKB:Q9BZQ4};
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:0000250|UniProtKB:Q9BZQ4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22861;
CC Evidence={ECO:0000250|UniProtKB:Q9BZQ4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22862;
CC Evidence={ECO:0000250|UniProtKB:Q9BZQ4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Divalent metal cations. Mg(2+) confers the highest activity.
CC {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC135388; AAI35389.1; -; mRNA.
DR RefSeq; NP_001096243.1; NM_001102773.1.
DR AlphaFoldDB; A4IH61; -.
DR SMR; A4IH61; -.
DR STRING; 8364.ENSXETP00000011433; -.
DR PaxDb; A4IH61; -.
DR DNASU; 100124800; -.
DR GeneID; 100124800; -.
DR KEGG; xtr:100124800; -.
DR CTD; 23057; -.
DR eggNOG; KOG3199; Eukaryota.
DR HOGENOM; CLU_033366_1_0_1; -.
DR InParanoid; A4IH61; -.
DR OMA; NECDMEV; -.
DR OrthoDB; 1308027at2759; -.
DR PhylomeDB; A4IH61; -.
DR TreeFam; TF315035; -.
DR Reactome; R-XTR-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00332.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012527; Expressed in brain and 6 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Golgi apparatus; NAD; Nucleotide-binding;
KW Nucleotidyltransferase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="Nicotinamide/nicotinic acid mononucleotide
FT adenylyltransferase 2"
FT /id="PRO_0000328664"
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 55..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 200..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 212..213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 271..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
SQ SEQUENCE 307 AA; 34362 MW; 2064FED4ADF38704 CRC64;
MAETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGK FIVIGGIISP VHDSYGKQGL
VSSRHRLNMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP
SVTPVIGQSL NQSTQPVYQN SNLSNKPTAV RILGKVGEGL SRMCCVRPNL QRVTFVDENA
NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNESDMEV IVGDFGIVVV PRDSVEPEQI
INHSSLLRKY KNNILTVKDD SNHPMAVVSS TKSRLALQHG DGHVVDYLAQ PVIDYVLKSQ
LYINTSG
