ID   NADD_GRAFK              Reviewed;         194 AA.
AC   A0M6X6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=GFO_3431;
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL68371.1; -; Genomic_DNA.
DR   RefSeq; WP_011711272.1; NC_008571.1.
DR   AlphaFoldDB; A0M6X6; -.
DR   SMR; A0M6X6; -.
DR   STRING; 411154.GFO_3431; -.
DR   EnsemblBacteria; CAL68371; CAL68371; GFO_3431.
DR   KEGG; gfo:GFO_3431; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_069765_3_3_10; -.
DR   OMA; IHIGHLI; -.
DR   OrthoDB; 1433958at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000000755; Chromosome.
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   3: Inferred from homology;
KW   ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..194
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000336695"
SQ   SEQUENCE   194 AA;  22608 MW;  1EC28218A5711F86 CRC64;
     MNRKVGLFFG TFNPIHTGHL IIANHMAEYS DLEEIWLVVT PHNPHKKKSS LLDNHHRLEM
     VYRACEGYGK LKPSNIEFDL PQPNYTVNTL AHIQEKFPTN DFCLIMGEDN LKSFHKWKNS
     EVIIENHEIY VYPRIAPGKV ADEFKTHAKI TRVAAPIIEI SSTFIRKSIK ESKNIGPLLD
     EKVWKYIDEM NFYK