NADD_ACIF2
ID NADD_ACIF2 Reviewed; 218 AA.
AC B7J9S1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=AFE_2948;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001219; ACK80555.1; -; Genomic_DNA.
DR RefSeq; WP_012537494.1; NC_011761.1.
DR AlphaFoldDB; B7J9S1; -.
DR SMR; B7J9S1; -.
DR STRING; 243159.AFE_2948; -.
DR PaxDb; B7J9S1; -.
DR EnsemblBacteria; ACK80555; ACK80555; AFE_2948.
DR GeneID; 66433888; -.
DR KEGG; afr:AFE_2948; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_0_0_6; -.
DR OMA; IHIGHLI; -.
DR OrthoDB; 1433958at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000001362; 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; Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_1000125332"
SQ SEQUENCE 218 AA; 24501 MW; B13544C526A7D2C7 CRC64;
MHSSTHDDLV ILGGTFDPIH YGHLRAVEEV RQALAIAQAM LIPAGHPPHR KSPWADARHR
LAMTRIAVAH HPQFTVSSWE VEREGPSYTV DTLTALRQQR PDAVLAMVIG MDAFLRFDTW
HHWQHILDLT HLVVTGRPGW PAAELPEALR QALYQRRCED VDALRQTPAG CILFHTVTAL
EISASNIRSL LAGHQSPRFL LPDEVLDYID AEGLYQSP
