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 03-AUG-2022, entry version 145.
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}.
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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 AlphaFoldDB; P54455; -.
DR SMR; P54455; -.
DR STRING; 224308.BSU25640; -.
DR DrugBank; DB04099; Deamido-Nad.
DR PaxDb; P54455; -.
DR PRIDE; P54455; -.
DR EnsemblBacteria; CAB14506; CAB14506; BSU_25640.
DR GeneID; 937818; -.
DR KEGG; bsu:BSU25640; -.
DR PATRIC; fig|224308.179.peg.2787; -.
DR eggNOG; COG1057; Bacteria.
DR InParanoid; P54455; -.
DR OMA; IHIGHLI; -.
DR PhylomeDB; P54455; -.
DR BioCyc; BSUB:BSU25640-MON; -.
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;
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:0007829|PDB:1KAM"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1KAQ"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1KAM"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1KAQ"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:1KAM"
FT TURN 107..112
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1KAQ"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1KAM"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1KAM"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:1KAM"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1KAM"
FT HELIX 175..183
FT /evidence="ECO:0007829|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
