ID C8X0X7_DESRD Unreviewed; 209 AA.
AC C8X0X7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 OrderedLocusNames=Dret_0782 {ECO:0000313|EMBL:ACV68074.1};
OS Desulfohalobium retbaense (strain ATCC 49708 / DSM 5692 / JCM 16813 /
OS HR100).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfohalobiaceae; Desulfohalobium.
OX NCBI_TaxID=485915 {ECO:0000313|EMBL:ACV68074.1, ECO:0000313|Proteomes:UP000001052};
RN [1] {ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|Proteomes:UP000001052};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Desulfohalobium retbaense DSM 5692.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACV68074.1, ECO:0000313|Proteomes:UP000001052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5692 {ECO:0000313|EMBL:ACV68074.1,
RC ECO:0000313|Proteomes:UP000001052};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
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; CP001734; ACV68074.1; -; Genomic_DNA.
DR RefSeq; WP_015751232.1; NC_013223.1.
DR AlphaFoldDB; C8X0X7; -.
DR STRING; 485915.Dret_0782; -.
DR KEGG; drt:Dret_0782; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_0_1_7; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000001052; 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; 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:ACV68074.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000001052};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:ACV68074.1}.
FT DOMAIN 5..184
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 209 AA; 23606 MW; EB98FBCCE2E4DFD9 CRC64;
MRVGVLGGSF NPVHIGHLRL ALEALAVENL DRVELVPAAV PPHKQNEILM PFSKRCELLE
AATHSIPELV VNPLEGQRQG PSYTVDTLRV FHASVAPEEL FFLLGCGDFL TLPHWYAWED
LLQLTNFCVV GRNGEGREAL RSFVEDHCQA KPLAEDLWQL PGASRRVRFL PIPRLDVSSS
LIRRYLRHDR SIRFLVPDCV VEVLEQGMQ
//
