NADM_PYRAB
ID NADM_PYRAB Reviewed; 186 AA.
AC Q9UYD4; G8ZIZ8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase;
DE EC=2.7.7.1;
DE AltName: Full=NAD(+) diphosphorylase;
DE AltName: Full=NAD(+) pyrophosphorylase;
DE AltName: Full=NMN adenylyltransferase;
GN OrderedLocusNames=PYRAB15740; ORFNames=PAB1318;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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 -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AJ248288; CAB50478.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71031.1; -; Genomic_DNA.
DR PIR; H75004; H75004.
DR RefSeq; WP_010868691.1; NC_000868.1.
DR AlphaFoldDB; Q9UYD4; -.
DR SMR; Q9UYD4; -.
DR STRING; 272844.PAB1318; -.
DR EnsemblBacteria; CAB50478; CAB50478; PAB1318.
DR GeneID; 1495860; -.
DR KEGG; pab:PAB1318; -.
DR PATRIC; fig|272844.11.peg.1678; -.
DR eggNOG; arCOG00972; Archaea.
DR HOGENOM; CLU_108783_0_0_2; -.
DR OMA; NSVWVSH; -.
DR OrthoDB; 90722at2157; -.
DR PhylomeDB; Q9UYD4; -.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
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; Transferase.
FT CHAIN 1..186
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_0000134998"
SQ SEQUENCE 186 AA; 21417 MW; E8230B688481386E CRC64;
MIRGLFVGRF QPVHKGHIKA LEFVFSQVDE VIIGIGSAQA SHTLKNPFTT GERMEMLIRA
IEEAGFKKRY YLVPLPDINF NAIWVPYVES MVPKFHVVFT GNSLVAQLFR ERGYKVVVQP
MFRKDILSAT EIRRRMIAGE PWEDLVPKSV VEYIKEIKGV ERLRNLATNL ESSEKELQAP
IRIPEF