NADM_HALMA
ID NADM_HALMA Reviewed; 188 AA.
AC Q5V117;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00243};
DE EC=2.7.7.1 {ECO:0000255|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00243};
DE AltName: Full=NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00243};
DE AltName: Full=NMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00243};
GN OrderedLocusNames=rrnAC1913;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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:0000255|HAMAP-Rule:MF_00243};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00243}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00243}.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00243}.
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DR EMBL; AY596297; AAV46786.1; -; Genomic_DNA.
DR RefSeq; WP_004958079.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V117; -.
DR SMR; Q5V117; -.
DR STRING; 272569.rrnAC1913; -.
DR EnsemblBacteria; AAV46786; AAV46786; rrnAC1913.
DR GeneID; 40152841; -.
DR GeneID; 64821552; -.
DR KEGG; hma:rrnAC1913; -.
DR PATRIC; fig|272569.17.peg.2570; -.
DR eggNOG; arCOG00972; Archaea.
DR HOGENOM; CLU_108783_0_0_2; -.
DR OMA; NSVWVSH; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02166; NMNAT_Archaea; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00243; NMN_adenylyltr; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR006418; NMN_Atrans_arc.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR01527; arch_NMN_Atrans; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..188
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_0000134989"
FT REGION 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 21482 MW; 2216E3B3AA641D85 CRC64;
MRGFYIGRFQ PYHNGHHSMV ERISEEVDEL VLGIGSADDS HTTHDPFTAG ERIMMITKAV
AEYDLTTYVV PLEDINRNAV WVSHVESMCP DFDVAYSNNP LVVRLFEEAG IEVRQSPMFD
RDRLEGSEIR QRMIDDESWR DRVPASVVEV IEEIHGIKRL QHVSDSDSLE RYAATGESLP
ESLDDLDD
