NADD_BACAC
ID NADD_BACAC Reviewed; 189 AA.
AC C3L5T6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE EC=2.7.7.18 {ECO:0000255|HAMAP-Rule:MF_00244};
DE AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE Short=NaMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
GN Name=nadD {ECO:0000255|HAMAP-Rule:MF_00244}; OrderedLocusNames=BAMEG_4595;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000255|HAMAP-Rule:MF_00244}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00244};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00244}.
CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000255|HAMAP-
CC Rule:MF_00244}.
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DR EMBL; CP001215; ACP12849.1; -; Genomic_DNA.
DR RefSeq; WP_001226053.1; NC_012581.1.
DR PDB; 2QTR; X-ray; 1.70 A; A/B/C=1-189.
DR PDB; 3MLA; X-ray; 1.75 A; A/B=1-189.
DR PDB; 3MLB; X-ray; 1.80 A; A/B=1-189.
DR PDB; 3MMX; X-ray; 2.55 A; A/B/C/D/E/F/G/H=1-189.
DR PDBsum; 2QTR; -.
DR PDBsum; 3MLA; -.
DR PDBsum; 3MLB; -.
DR PDBsum; 3MMX; -.
DR AlphaFoldDB; C3L5T6; -.
DR SMR; C3L5T6; -.
DR BindingDB; C3L5T6; -.
DR ChEMBL; CHEMBL1075320; -.
DR KEGG; bah:BAMEG_4595; -.
DR HOGENOM; CLU_069765_3_1_9; -.
DR OMA; IHIGHLI; -.
DR BRENDA; 2.7.7.18; 634.
DR UniPathway; UPA00253; UER00332.
DR EvolutionaryTrace; C3L5T6; -.
DR PRO; PR:C3L5T6; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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; Transferase.
FT CHAIN 1..189
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_1000125337"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3MLA"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3MLA"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2QTR"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:2QTR"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:2QTR"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:2QTR"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2QTR"
SQ SEQUENCE 189 AA; 21955 MW; A26101CCE8549C53 CRC64;
MRKIGIIGGT FDPPHYGHLL IANEVYHALN LEEVWFLPNQ IPPHKQGRNI TSVESRLQML
ELATEAEEHF SICLEELSRK GPSYTYDTML QLTKKYPDVQ FHFIIGGDMV EYLPKWYNIE
ALLDLVTFVG VARPGYKLRT PYPITTVEIP EFAVSSSLLR ERYKEKKTCK YLLPEKVQVY
IERNGLYES
