ID F8AB95_THEID Unreviewed; 211 AA.
AC F8AB95;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=Thein_1695 {ECO:0000313|EMBL:AEH45553.1};
OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator.
OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH45553.1, ECO:0000313|Proteomes:UP000006793};
RN [1] {ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEH45553.1, ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RX PubMed=22768359; DOI=10.4056/sigs.2665915;
RA Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL Stand. Genomic Sci. 6:155-164(2012).
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; CP002683; AEH45553.1; -; Genomic_DNA.
DR RefSeq; WP_013908294.1; NC_015681.1.
DR AlphaFoldDB; F8AB95; -.
DR STRING; 667014.Thein_1695; -.
DR PaxDb; 667014-Thein_1695; -.
DR KEGG; tid:Thein_1695; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_3_1_0; -.
DR InParanoid; F8AB95; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000006793; 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:AEH45553.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000006793};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:AEH45553.1}.
FT DOMAIN 6..183
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 211 AA; 24429 MW; 52EAF8C80E1E8FF4 CRC64;
MERVGLLGGT FDPIHLGHLR AGLEVYEKLA LSKLVFIPAG TPPHKKRRPL SPFSLRYEMT
KLAIKDTPYF EVSDIEGRRQ GPSYSVLTLE ELKTVSKYEF FFILGLDAYL EFDIWYQYQR
IPELAHVVVI NRGPGGQKEF FEKTRKIFPQ AQEKEGIFHL PKGKSLRFLP VTRLDISSTM
IREAVKTRKS IQFLVPESVR EFIALHKLYL D
//
