ID S4RNG9_PETMA Unreviewed; 307 AA.
AC S4RNG9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000006755.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000006755.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; S4RNG9; -.
DR STRING; 7757.ENSPMAP00000006755; -.
DR Ensembl; ENSPMAT00000006785.1; ENSPMAP00000006755.1; ENSPMAG00000006094.1.
DR GeneTree; ENSGT00950000183179; -.
DR HOGENOM; CLU_033366_1_0_1; -.
DR OMA; QPWKENI; -.
DR OrthoDB; 5488885at2759; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000245300; Unplaced.
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:UP000245300}.
FT DOMAIN 12..99
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 34584 MW; F98752DFBA8F14AE CRC64;
MSEQTKTHVI LLACGSFNPV TKGHLQMFED ARDYLHKSGR FIVIGGIISP VHDGYRKQGL
ISSRHRLSMC QLAVQNSDWI RVDPWECYQE KWQTTCDVLE HHRELMKRVT GCILSNVNSP
SSPVIKQPHN ETRPATQDAN SVPLQKSTPG KLISKFGESI GKVCCLRPKA DLFPYIDENA
NLGNSVRYEE IELRIMLLCG SDLLESFSIP GLWNDDDLKV ILAEFGVVCV PRDCADSERI
IRRSRHLLKF KKNINVVNDA VDGPTAHISS TKSRLALQKG DGRVSEYLSQ PVIDYILQHQ
LYINTSG
//
