(data stored in SCRATCH zone)

SWISSPROT: NADD_BACSU

ID   NADD_BACSU              Reviewed;         189 AA.
AC   P54455;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 135.
DE   RecName: Full=Nicotinate-nucleotide adenylyltransferase;
DE            EC=2.7.7.18;
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=yqeJ; OrderedLocusNames=BSU25640;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=11704676; DOI=10.1074/jbc.m109670200;
RA   Olland A.M., Underwood K.W., Czerwinski R.M., Lo M.-C., Aulabaugh A.,
RA   Bard J., Stahl M.L., Somers W.S., Sullivan F.X., Chopra R.;
RT   "Identification, characterization, and crystal structure of Bacillus
RT   subtilis nicotinic acid mononucleotide adenylyltransferase.";
RL   J. Biol. Chem. 277:3698-3707(2002).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}.
DR   EMBL; D84432; BAA12447.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14506.1; -; Genomic_DNA.
DR   PIR; F69951; F69951.
DR   RefSeq; NP_390442.1; NC_000964.3.
DR   RefSeq; WP_004398676.1; NZ_JNCM01000036.1.
DR   PDB; 1KAM; X-ray; 2.10 A; A/B/C/D=2-189.
DR   PDB; 1KAQ; X-ray; 3.20 A; A/B/C/D/E/F=2-189.
DR   PDBsum; 1KAM; -.
DR   PDBsum; 1KAQ; -.
DR   SMR; P54455; -.
DR   STRING; 224308.BSU25640; -.
DR   DrugBank; DB04099; Deamido-Nad+.
DR   PaxDb; P54455; -.
DR   PRIDE; P54455; -.
DR   EnsemblBacteria; CAB14506; CAB14506; BSU25640.
DR   GeneID; 937818; -.
DR   KEGG; bsu:BSU25640; -.
DR   PATRIC; fig|224308.179.peg.2787; -.
DR   eggNOG; ENOG4108Z1W; Bacteria.
DR   eggNOG; COG1057; LUCA.
DR   HOGENOM; HOG000262780; -.
DR   InParanoid; P54455; -.
DR   KO; K00969; -.
DR   OMA; IHIGHLI; -.
DR   PhylomeDB; P54455; -.
DR   BioCyc; BSUB:BSU25640-MONOMER; -.
DR   BRENDA; 2.7.7.18; 658.
DR   UniPathway; UPA00253; UER00332.
DR   EvolutionaryTrace; P54455; -.
DR   Proteomes; UP000001570; 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; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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;
DR   PRODOM; P54455.
DR   SWISS-2DPAGE; P54455.
KW   3D-structure; ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..189
FT                   /note="Nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181387"
FT   STRAND          3..9
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   HELIX           16..28
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          32..38
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          46..48
FT                   /evidence="ECO:0000244|PDB:1KAQ"
FT   HELIX           53..64
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          70..72
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   HELIX           75..77
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          78..81
FT                   /evidence="ECO:0000244|PDB:1KAQ"
FT   HELIX           85..95
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          99..106
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   TURN            107..112
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          113..116
FT                   /evidence="ECO:0000244|PDB:1KAQ"
FT   HELIX           117..125
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          126..132
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   STRAND          145..148
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   HELIX           156..165
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   TURN            170..172
FT                   /evidence="ECO:0000244|PDB:1KAM"
FT   HELIX           175..183
FT                   /evidence="ECO:0000244|PDB:1KAM"
SQ   SEQUENCE   189 AA;  22157 MW;  E2383AA7F0624B95 CRC64;
     MKKIGIFGGT FDPPHNGHLL MANEVLYQAG LDEIWFMPNQ IPPHKQNEDY TDSFHRVEML
     KLAIQSNPSF KLELVEMERE GPSYTFDTVS LLKQRYPNDQ LFFIIGADMI EYLPKWYKLD
     ELLNLIQFIG VKRPGFHVET PYPLLFADVP EFEVSSTMIR ERFKSKKPTD YLIPDKVKKY
     VEENGLYES
//

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