NADD_ECOLI
ID NADD_ECOLI Reviewed; 213 AA.
AC P0A752; P52085;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Nicotinate-nucleotide adenylyltransferase;
DE EC=2.7.7.18 {ECO:0000269|PubMed:10894752};
DE AltName: Full=Deamido-NAD(+) diphosphorylase;
DE AltName: Full=Deamido-NAD(+) pyrophosphorylase;
DE AltName: Full=Nicotinate mononucleotide adenylyltransferase;
DE Short=NaMN adenylyltransferase;
GN Name=nadD; Synonyms=ybeN; OrderedLocusNames=b0639, JW0634;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Addinall S.G., Donachie W.D.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=B;
RX PubMed=10894752; DOI=10.1128/jb.182.15.4372-4374.2000;
RA Mehl R.A., Kinsland C., Begley T.P.;
RT "Identification of the Escherichia coli nicotinic acid mononucleotide
RT adenylyltransferase gene.";
RL J. Bacteriol. 182:4372-4374(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11796112; DOI=10.1016/s0969-2126(01)00693-1;
RA Zhang H., Zhou T., Kurnasov O., Cheek S., Grishin N.V., Osterman A.;
RT "Crystal structures of E. coli nicotinate mononucleotide
RT adenylyltransferase and its complex with deamido-NAD.";
RL Structure 10:69-79(2002).
CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000269|PubMed:10894752}.
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:0000269|PubMed:10894752};
CC -!- ACTIVITY REGULATION: Activity is susceptible to product inhibition.
CC {ECO:0000269|PubMed:10894752}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}.
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DR EMBL; U23163; AAA64852.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40840.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73740.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35286.1; -; Genomic_DNA.
DR PIR; E64798; E64798.
DR RefSeq; NP_415172.1; NC_000913.3.
DR RefSeq; WP_000838889.1; NZ_STEB01000031.1.
DR PDB; 1K4K; X-ray; 2.00 A; A/B/C/D=1-213.
DR PDB; 1K4M; X-ray; 1.90 A; A/B/C=1-213.
DR PDB; 6KG3; X-ray; 3.08 A; A/B/C/D/E/F=1-213.
DR PDB; 6KH2; X-ray; 3.04 A; A/B/C/D/E/F=1-213.
DR PDBsum; 1K4K; -.
DR PDBsum; 1K4M; -.
DR PDBsum; 6KG3; -.
DR PDBsum; 6KH2; -.
DR AlphaFoldDB; P0A752; -.
DR SMR; P0A752; -.
DR IntAct; P0A752; 7.
DR STRING; 511145.b0639; -.
DR BindingDB; P0A752; -.
DR ChEMBL; CHEMBL3638351; -.
DR jPOST; P0A752; -.
DR PaxDb; P0A752; -.
DR PRIDE; P0A752; -.
DR EnsemblBacteria; AAC73740; AAC73740; b0639.
DR EnsemblBacteria; BAA35286; BAA35286; BAA35286.
DR GeneID; 66671087; -.
DR GeneID; 945248; -.
DR KEGG; ecj:JW0634; -.
DR KEGG; eco:b0639; -.
DR PATRIC; fig|1411691.4.peg.1629; -.
DR EchoBASE; EB3030; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_0_0_6; -.
DR InParanoid; P0A752; -.
DR OMA; IHIGHLI; -.
DR PhylomeDB; P0A752; -.
DR BioCyc; EcoCyc:NICONUCADENYLYLTRAN-MON; -.
DR BioCyc; MetaCyc:NICONUCADENYLYLTRAN-MON; -.
DR BRENDA; 2.7.7.1; 2026.
DR BRENDA; 2.7.7.18; 2026.
DR UniPathway; UPA00253; UER00332.
DR EvolutionaryTrace; P0A752; -.
DR PRO; PR:P0A752; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IMP:EcoCyc.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR GO; GO:0034355; P:NAD salvage; IMP:EcoCyc.
DR CDD; cd02165; NMNAT; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00244; NaMN_adenylyltr; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="Nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000181407"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6KH2"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1K4K"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1K4M"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1K4M"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:1K4M"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:1K4M"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1K4M"
SQ SEQUENCE 213 AA; 24528 MW; EA2C675282400CF5 CRC64;
MKSLQALFGG TFDPVHYGHL KPVETLANLI GLTRVTIIPN NVPPHRPQPE ANSVQRKHML
ELAIADKPLF TLDERELKRN APSYTAQTLK EWRQEQGPDV PLAFIIGQDS LLTFPTWYEY
ETILDNAHLI VCRRPGYPLE MAQPQYQQWL EDHLTHNPED LHLQPAGKIY LAETPWFNIS
ATIIRERLQN GESCEDLLPE PVLTYINQQG LYR
