NADD_DINSH
ID NADD_DINSH Reviewed; 195 AA.
AC A8LR16;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Dshi_2203;
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
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; CP000830; ABV93939.1; -; Genomic_DNA.
DR RefSeq; WP_012178870.1; NC_009952.1.
DR AlphaFoldDB; A8LR16; -.
DR SMR; A8LR16; -.
DR STRING; 398580.Dshi_2203; -.
DR EnsemblBacteria; ABV93939; ABV93939; Dshi_2203.
DR KEGG; dsh:Dshi_2203; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_2_0_5; -.
DR OMA; IHIGHLI; -.
DR OrthoDB; 1433958at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000006833; 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; TIGR00482; TIGR00482; 1.
PE 3: Inferred from homology;
KW ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..195
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_1000078380"
SQ SEQUENCE 195 AA; 21311 MW; 78A65AC65C36AFED CRC64;
MRSGWPMAGT GQTVGLLGGS FDPAHGGHVH ITRQALARFG LDWVWWLVSP GNPLKPNPPA
PLALRCARAR ALMRHPRVRI TGIEAELGTR YTAETVAGLR RCYPGVRFVW LMGADNLAQF
HRWDRWDEIM AQVPVGVLAR PGQRLAALRA PAAQRFAGAR RGAAGLGRAQ APAWAFVNVP
LVDLSSSEIR ARGDW