ID C2CFN7_9FIRM Unreviewed; 198 AA.
AC C2CFN7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:EEI83568.1};
GN ORFNames=HMPREF0077_0297 {ECO:0000313|EMBL:EEI83568.1};
OS Anaerococcus tetradius ATCC 35098.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525255 {ECO:0000313|EMBL:EEI83568.1, ECO:0000313|Proteomes:UP000003744};
RN [1] {ECO:0000313|EMBL:EEI83568.1, ECO:0000313|Proteomes:UP000003744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35098 {ECO:0000313|EMBL:EEI83568.1,
RC ECO:0000313|Proteomes:UP000003744};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEI83568.1}.
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DR EMBL; ACGC01000013; EEI83568.1; -; Genomic_DNA.
DR RefSeq; WP_004835993.1; NZ_GG666295.1.
DR AlphaFoldDB; C2CFN7; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_0_1_9; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000003744; 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:EEI83568.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:EEI83568.1}.
FT DOMAIN 5..171
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 198 AA; 23163 MW; 3FCC37C565F71957 CRC64;
MRIGLYGGTF DPIHTGHLIV IENAINFMKL DKVIILPSSN PPHKKNKKKT DTNIRVEMVS
EAIKDNDKIV LSTFESTDDT IRYTHETIRY FKEKFNKDDV FYIMGEDSFL TIDTWKNYKD
ILGEKIIVFT RSNIDKDSEL VRKVDEIRKD NPNIFLINNL NINISSTLIR QLVKDRLSIK
YLVSDNVKYI IEKRGLYV
//
