NADE_BACAN
ID NADE_BACAN Reviewed; 272 AA.
AC Q81RP3; Q6HZW9; Q6KTU9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193};
DE EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193};
GN Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193};
GN OrderedLocusNames=BA_1998, GBAA_1998, BAS1855;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:2PZ8, ECO:0007744|PDB:2PZA, ECO:0007744|PDB:2PZB}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEXES WITH AMP; DIPHOSPHATE
RP AND SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=17642516; DOI=10.1107/s0907444907029769;
RA McDonald H.M., Pruett P.S., Deivanayagam C., Protasevich I.I., Carson W.M.,
RA DeLucas L.J., Brouillette W.J., Brouillette C.G.;
RT "Structural adaptation of an interacting non-native C-terminal helical
RT extension revealed in the crystal structure of NAD+ synthetase from
RT Bacillus anthracis.";
RL Acta Crystallogr. D 63:891-905(2007).
CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC Rule:MF_00193, ECO:0000269|PubMed:17642516}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00193,
CC ECO:0000269|PubMed:17642516};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=289 uM for ATP {ECO:0000269|PubMed:17642516};
CC KM=152 uM for deamido-NAD(+) {ECO:0000269|PubMed:17642516};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:17642516};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193,
CC ECO:0000269|PubMed:17642516}.
CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC Rule:MF_00193}.
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DR EMBL; AE016879; AAP25889.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT31119.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT54170.1; -; Genomic_DNA.
DR RefSeq; NP_844403.1; NC_003997.3.
DR RefSeq; WP_000174879.1; NZ_WXXJ01000029.1.
DR RefSeq; YP_028119.1; NC_005945.1.
DR PDB; 2PZ8; X-ray; 2.00 A; A/B=1-272.
DR PDB; 2PZA; X-ray; 2.40 A; A/B=1-272.
DR PDB; 2PZB; X-ray; 1.90 A; A/B/C/D=1-272.
DR PDBsum; 2PZ8; -.
DR PDBsum; 2PZA; -.
DR PDBsum; 2PZB; -.
DR AlphaFoldDB; Q81RP3; -.
DR SMR; Q81RP3; -.
DR STRING; 260799.BAS1855; -.
DR BindingDB; Q81RP3; -.
DR ChEMBL; CHEMBL5271; -.
DR DNASU; 1087061; -.
DR EnsemblBacteria; AAP25889; AAP25889; BA_1998.
DR EnsemblBacteria; AAT31119; AAT31119; GBAA_1998.
DR GeneID; 64202633; -.
DR KEGG; ban:BA_1998; -.
DR KEGG; bar:GBAA_1998; -.
DR KEGG; bat:BAS1855; -.
DR PATRIC; fig|198094.11.peg.1971; -.
DR eggNOG; COG0171; Bacteria.
DR HOGENOM; CLU_059327_3_0_9; -.
DR OMA; MAFLYDY; -.
DR BRENDA; 6.3.1.5; 634.
DR UniPathway; UPA00253; UER00333.
DR EvolutionaryTrace; Q81RP3; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Magnesium; Metal-binding; NAD;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..272
FT /note="NH(3)-dependent NAD(+) synthetase"
FT /id="PRO_0000152156"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 138
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 171
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 178
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193,
FT ECO:0000305|PubMed:17642516"
FT BINDING 258..259
FT /ligand="deamido-NAD(+)"
FT /ligand_id="ChEBI:CHEBI:58437"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00193"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:2PZB"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 50..68
FT /evidence="ECO:0007829|PDB:2PZB"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2PZB"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2PZ8"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:2PZB"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 129..151
FT /evidence="ECO:0007829|PDB:2PZB"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:2PZB"
FT TURN 171..175
FT /evidence="ECO:0007829|PDB:2PZ8"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2PZ8"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2PZB"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2PZ8"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:2PZ8"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:2PZB"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:2PZ8"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:2PZB"
SQ SEQUENCE 272 AA; 30101 MW; B58A9792E8075B98 CRC64;
MTLQEQIMKA LHVQPVIDPK AEIRKRVDFL KDYVKKTGAK GFVLGISGGQ DSTLAGRLAQ
LAVEEIRNEG GNATFIAVRL PYKVQKDEDD AQLALQFIQA DQSVAFDIAS TVDAFSNQYE
NLLDESLTDF NKGNVKARIR MVTQYAIGGQ KGLLVIGTDH AAEAVTGFFT KFGDGGADLL
PLTGLTKRQG RALLQELGAD ERLYLKMPTA DLLDEKPGQA DETELGITYD QLDDYLEGKT
VPADVAEKIE KRYTVSEHKR QVPASMFDDW WK
