NADD_GLUDA
ID NADD_GLUDA Reviewed; 215 AA.
AC A9HC14; B5ZGF8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 76.
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};
GN OrderedLocusNames=GDI0941, Gdia_1083;
OS Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS / CIP 103539 / LMG 7603 / PAl5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=272568;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A.,
RA Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA Figueiredo D., Montano H., Junior J., de Souza Filho G.,
RA Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P.,
RA Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M.,
RA Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A.,
RA Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T.,
RA Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O.,
RA Baldani J.I., Ferreira P.C.;
RT "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT Gluconacetobacter diazotrophicus Pal5.";
RL BMC Genomics 10:450-450(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 / PAl5;
RX PubMed=21304715; DOI=10.4056/sigs.972221;
RA Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.;
RT "Two genome sequences of the same bacterial strain, Gluconacetobacter
RT diazotrophicus PAl 5, suggest a new standard in genome sequence
RT submission.";
RL Stand. Genomic Sci. 2:309-317(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACI50866.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=ACI50866.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM889285; CAP54884.1; -; Genomic_DNA.
DR EMBL; CP001189; ACI50866.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; WP_012223796.1; NC_010125.1.
DR AlphaFoldDB; A9HC14; -.
DR SMR; A9HC14; -.
DR STRING; 272568.GDI0941; -.
DR EnsemblBacteria; ACI50866; ACI50866; Gdia_1083.
DR EnsemblBacteria; CAP54884; CAP54884; GDI0941.
DR KEGG; gdi:GDI0941; -.
DR KEGG; gdj:Gdia_1083; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_688428_0_0_5; -.
DR OMA; IHIGHLI; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000000736; Chromosome.
DR Proteomes; UP000001176; 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.
PE 3: Inferred from homology;
KW ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..215
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000336694"
FT CONFLICT 5
FT /note="A -> P (in Ref. 2; ACI50866)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="V -> L (in Ref. 2; ACI50866)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="H -> Q (in Ref. 2; ACI50866)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="I -> V (in Ref. 2; ACI50866)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Y -> N (in Ref. 2; ACI50866)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="F -> V (in Ref. 2; ACI50866)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 24049 MW; 254A4D11BFA86B79 CRC64;
MSSIAAWGDG RRTRIGVLGG SFNPVHDGHL QLARRALRHL RLDQVWLMIS PGYPLKPVQG
MAPFDVRLAS VAARFDGRRL VATDIERRLG TRYTVDTLGL LRLRFPHAAF VWLMGADGLA
DLARWRDWRR IVSLVPFAVL PRPTYNPGAL RGEAAVALAR WRRPARQAPI LADCAPCAWA
FLPAPQIGIS ATELRASALR QRSRHPTHKH TTHQE
