NADM_METTH
ID NADM_METTH Reviewed; 178 AA.
AC O26253;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 135.
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=MTH_150;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11017201; DOI=10.1038/82823;
RA Christendat D., Yee A., Dharamsi A., Kluger Y., Savchenko A., Cort J.R.,
RA Booth V., Mackereth C.D., Saridakis V., Ekiel I., Kozlov G., Maxwell K.L.,
RA Wu N., McIntosh L.P., Gehring K., Kennedy M.A., Davidson A.R., Pai E.F.,
RA Gerstein M., Edwards A.M., Arrowsmith C.H.;
RT "Structural proteomics of an archaeon.";
RL Nat. Struct. Biol. 7:903-909(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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB84656.1; ALT_INIT; Genomic_DNA.
DR PIR; A69067; A69067.
DR RefSeq; WP_048060754.1; NC_000916.1.
DR PDB; 1EJ2; X-ray; 1.90 A; A=1-178.
DR PDB; 1HYB; X-ray; 2.00 A; A=1-178.
DR PDB; 1M8F; X-ray; 2.40 A; A=1-178.
DR PDB; 1M8G; X-ray; 2.00 A; A=1-178.
DR PDB; 1M8J; X-ray; 2.40 A; A=1-178.
DR PDB; 1M8K; X-ray; 3.00 A; A/B/C=1-178.
DR PDB; 4YP5; X-ray; 2.21 A; A/B/C=1-178.
DR PDB; 4YP6; X-ray; 1.90 A; A/B/C=1-178.
DR PDB; 4YP7; X-ray; 2.30 A; A/B/C=1-178.
DR PDBsum; 1EJ2; -.
DR PDBsum; 1HYB; -.
DR PDBsum; 1M8F; -.
DR PDBsum; 1M8G; -.
DR PDBsum; 1M8J; -.
DR PDBsum; 1M8K; -.
DR PDBsum; 4YP5; -.
DR PDBsum; 4YP6; -.
DR PDBsum; 4YP7; -.
DR AlphaFoldDB; O26253; -.
DR SMR; O26253; -.
DR STRING; 187420.MTH_150; -.
DR PRIDE; O26253; -.
DR EnsemblBacteria; AAB84656; AAB84656; MTH_150.
DR GeneID; 1470111; -.
DR KEGG; mth:MTH_150; -.
DR PATRIC; fig|187420.15.peg.122; -.
DR HOGENOM; CLU_108783_0_0_2; -.
DR OMA; NSVWVSH; -.
DR BRENDA; 2.7.7.1; 3256.
DR SABIO-RK; O26253; -.
DR UniPathway; UPA00253; UER00600.
DR EvolutionaryTrace; O26253; -.
DR Proteomes; UP000005223; 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; NAD; Nucleotide-binding;
KW Nucleotidyltransferase; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..178
FT /note="Nicotinamide-nucleotide adenylyltransferase"
FT /id="PRO_0000134995"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1EJ2"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1EJ2"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:1EJ2"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1EJ2"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:1EJ2"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1EJ2"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4YP6"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:1EJ2"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:1EJ2"
SQ SEQUENCE 178 AA; 20207 MW; A1B4F41BA3FF98AE CRC64;
MRGLLVGRMQ PFHRGHLQVI KSILEEVDEL IICIGSAQLS HSIRDPFTAG ERVMMLTKAL
SENGIPASRY YIIPVQDIEC NALWVGHIKM LTPPFDRVYS GNPLVQRLFS EDGYEVTAPP
LFYRDRYSGT EVRRRMLDDG DWRSLLPESV VEVIDEINGV ERIKHLAKKE VSELGGIS
