NADM_METJA
ID NADM_METJA Reviewed; 168 AA.
AC Q57961;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 130.
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=MJ0541;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-6, AND CHARACTERIZATION.
RX PubMed=9401030; DOI=10.1128/jb.179.24.7718-7723.1997;
RA Raffaelli N., Pisani F.M., Lorenzi T., Emanuelli M., Amici A., Ruggieri S.,
RA Magni G.;
RT "Characterization of nicotinamide mononucleotide adenylyltransferase from
RT thermophilic archaea.";
RL J. Bacteriol. 179:7718-7723(1997).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10331644; DOI=10.1023/a:1006968328186;
RA Raffaelli N., Emanuelli M., Pisani F.M., Amici A., Lorenzi T., Ruggieri S.,
RA Magni G.;
RT "Identification of the archaeal NMN adenylytransferase gene.";
RL Mol. Cell. Biochem. 193:99-102(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
RX PubMed=10986466; DOI=10.1016/s0969-2126(00)00190-8;
RA D'Angelo I., Raffaelli N., Dabusti V., Lorenzi T., Magni G., Rizzi M.;
RT "Structure of nicotinamide mononucleotide adenylyltransferase: a key enzyme
RT in NAD(+) biosynthesis.";
RL Structure 8:993-1004(2000).
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 -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98533.1; -; Genomic_DNA.
DR PIR; E64367; E64367.
DR RefSeq; WP_010870045.1; NC_000909.1.
DR PDB; 1F9A; X-ray; 2.00 A; A/B/C/D/E/F=2-168.
DR PDBsum; 1F9A; -.
DR AlphaFoldDB; Q57961; -.
DR SMR; Q57961; -.
DR STRING; 243232.MJ_0541; -.
DR PRIDE; Q57961; -.
DR EnsemblBacteria; AAB98533; AAB98533; MJ_0541.
DR GeneID; 1451406; -.
DR KEGG; mja:MJ_0541; -.
DR eggNOG; arCOG00972; Archaea.
DR HOGENOM; CLU_108783_0_0_2; -.
DR InParanoid; Q57961; -.
DR OMA; NSVWVSH; -.
DR OrthoDB; 90722at2157; -.
DR PhylomeDB; Q57961; -.
DR BRENDA; 2.7.7.1; 3260.
DR UniPathway; UPA00253; UER00600.
DR EvolutionaryTrace; Q57961; -.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; NAD;
KW Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:9401030"
FT CHAIN 2..168
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_0000134992"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1F9A"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1F9A"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1F9A"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:1F9A"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:1F9A"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:1F9A"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1F9A"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:1F9A"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1F9A"
SQ SEQUENCE 168 AA; 19610 MW; D82FF45E68E29834 CRC64;
MRGFIIGRFQ PFHKGHLEVI KKIAEEVDEI IIGIGSAQKS HTLENPFTAG ERILMITQSL
KDYDLTYYPI PIKDIEFNSI WVSYVESLTP PFDIVYSGNP LVRVLFEERG YEVKRPEMFN
RKEYSGTEIR RRMLNGEKWE HLVPKAVVDV IKEIKGVERL RKLAQTDK
