ID A0A2K9EGZ2_9FIRM Unreviewed; 203 AA.
AC A0A2K9EGZ2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE EC=2.7.7.18 {ECO:0000256|HAMAP-Rule:MF_00244};
DE AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00244};
DE AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
DE Short=NaMN adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00244};
GN Name=nadD {ECO:0000256|HAMAP-Rule:MF_00244,
GN ECO:0000313|EMBL:AUG57193.1};
GN ORFNames=B9R14_10750 {ECO:0000313|EMBL:PQQ67176.1}, HVS_06335
GN {ECO:0000313|EMBL:AUG57193.1};
OS Acetivibrio saccincola.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=1677857 {ECO:0000313|EMBL:AUG57193.1, ECO:0000313|Proteomes:UP000233534};
RN [1] {ECO:0000313|EMBL:AUG57193.1, ECO:0000313|Proteomes:UP000233534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GGR1 {ECO:0000313|EMBL:AUG57193.1}, and SR1
RC {ECO:0000313|Proteomes:UP000233534};
RA Pechtl A., Ruckert C., Koeck D.E., Maus I., Winkler A., Kalinowski J.,
RA Puhler A., Schwarz W.W., Zverlov V.V., Schluter A., Liebl W.;
RT "Complete genome sequence of Herbivorax saccincola GGR1, a novel
RT Cellulosome-producing hydrolytic bacterium in a thermophilic biogas plant,
RT established by Illumina and Nanopore MinION sequencing.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PQQ67176.1, ECO:0000313|Proteomes:UP000239720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7 {ECO:0000313|EMBL:PQQ67176.1,
RC ECO:0000313|Proteomes:UP000239720};
RX PubMed=29482868; DOI=10.1016/j.syapm.2018.01.010;
RA Aikawa S., Baramee S., Sermsathanaswadi J., Thianheng P., Tachaapaikoon C.,
RA Shikata A., Waeonukul R., Pason P., Ratanakhanokchai K., Kosugi A.;
RT "Characterization and high-quality draft genome sequence of Herbivorax
RT saccincola A7, an anaerobic, alkaliphilic, thermophilic, cellulolytic, and
RT xylanolytic bacterium.";
RL Syst. Appl. Microbiol. 41:261-269(2018).
CC -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC {ECO:0000256|ARBA:ARBA00002324, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001785, ECO:0000256|HAMAP-
CC Rule:MF_00244};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005019, ECO:0000256|HAMAP-Rule:MF_00244}.
CC -!- SIMILARITY: Belongs to the NadD family. {ECO:0000256|HAMAP-
CC Rule:MF_00244}.
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DR EMBL; CP025197; AUG57193.1; -; Genomic_DNA.
DR EMBL; NEMB01000003; PQQ67176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9EGZ2; -.
DR KEGG; hsc:HVS_06335; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000233534; Chromosome.
DR Proteomes; UP000239720; Unassembled WGS sequence.
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; HUPs; 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 NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR00482; nicotinate (nicotinamide) nucleotide adenylyltransferase; 1.
DR PANTHER; PTHR39321; NICOTINATE-NUCLEOTIDE ADENYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR39321:SF3; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00244};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00244};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW ECO:0000313|EMBL:AUG57193.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000233534};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:AUG57193.1}.
FT DOMAIN 8..177
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 203 AA; 23730 MW; 1F956820981831F1 CRC64;
MLTTKIGILG GTFNPIHNGH LIMAEEIRET FRLDKVLFMP SGNPPHKTGG EVIDKEHRFN
MVCEAVKGND FFEESRIEVE REGYTYTIDT LRKLKTLLKD NVLLYYIVGA DVLYDLSKWK
DFELVFRECE FIAALRPGFE SEGFEGHIKY LETKYHAKIK KAYIPLIDIS STEIRKRVKE
GRSIKYLVPE RVEKYIKENK LYL
//
