ID A0A3P8ZVU1_ESOLU Unreviewed; 308 AA.
AC A0A3P8ZVU1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 {ECO:0000256|ARBA:ARBA00040700};
DE EC=2.7.7.1 {ECO:0000256|ARBA:ARBA00012390};
DE EC=2.7.7.18 {ECO:0000256|ARBA:ARBA00012389};
DE AltName: Full=Nicotinamide mononucleotide adenylyltransferase 2 {ECO:0000256|ARBA:ARBA00041585};
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 2 {ECO:0000256|ARBA:ARBA00043172};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000032428.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000032428.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000032428.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004658}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005019}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004594}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004594}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00037794}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00037794}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00007064}.
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DR RefSeq; XP_010881581.1; XM_010883279.3.
DR AlphaFoldDB; A0A3P8ZVU1; -.
DR STRING; 8010.ENSELUP00000032428; -.
DR Ensembl; ENSELUT00000003243.2; ENSELUP00000032428.1; ENSELUG00000010331.2.
DR GeneID; 105018116; -.
DR KEGG; els:105018116; -.
DR GeneTree; ENSGT00950000183179; -.
DR InParanoid; A0A3P8ZVU1; -.
DR OMA; QPWKENI; -.
DR OrthoDB; 5488885at2759; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000265140; LG03.
DR Bgee; ENSELUG00000010331; Expressed in brain and 7 other cell types or tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:InterPro.
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; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR12039; NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR12039:SF18; NICOTINAMIDE_NICOTINIC ACID MONONUCLEOTIDE ADENYLYLTRANSFERASE 2; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT DOMAIN 14..106
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 308 AA; 34761 MW; 9B68BE4B77F6AC56 CRC64;
MTENTKTHVI LLSCGSFNPI TKGHIHMFEK AREYLHKTGK FIVIGGIISP VHDSYGKPGL
VPSRHRLTMC QLAVQSSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP
SSTPVIGQPR NDTQNTIYQN HNTNNNKPTA TKLWGKMSES LGKICCVRPH IDRFTFVDEN
ANLGTAMRYE EIELRILLLC GSDLLESFCI PGLWKDSDME VIVGDFGIVV VPRDGVDTER
IMNHSSVLRK YKDNIIVVKD DVNHPMSIVS STKSRLALQH GDGHVVDYLN QPVIDYILQS
QLYINASG
//
