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Database: UniProt
Entry: C2KVZ0_9FIRM
LinkDB: C2KVZ0_9FIRM
Original site: C2KVZ0_9FIRM 
ID   C2KVZ0_9FIRM            Unreviewed;        83 AA.
AC   C2KVZ0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=nicotinate-nucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012389};
DE            EC=2.7.7.18 {ECO:0000256|ARBA:ARBA00012389};
DE   Flags: Fragment;
GN   ORFNames=HMPREF6123_0659 {ECO:0000313|EMBL:EEJ52077.1};
OS   Oribacterium sinus F0268.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=585501 {ECO:0000313|EMBL:EEJ52077.1, ECO:0000313|Proteomes:UP000004121};
RN   [1] {ECO:0000313|EMBL:EEJ52077.1, ECO:0000313|Proteomes:UP000004121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0268 {ECO:0000313|EMBL:EEJ52077.1,
RC   ECO:0000313|Proteomes:UP000004121};
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 (APR-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}.
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};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005019}.
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:EEJ52077.1}.
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DR   EMBL; ACKX01000068; EEJ52077.1; -; Genomic_DNA.
DR   AlphaFoldDB; C2KVZ0; -.
DR   STRING; 585501.HMPREF6123_0659; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_2547952_0_0_9; -.
DR   InParanoid; C2KVZ0; -.
DR   OrthoDB; 5295945at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000004121; Unassembled WGS sequence.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02165; NMNAT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:EEJ52077.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004121};
KW   Transferase {ECO:0000313|EMBL:EEJ52077.1}.
FT   DOMAIN          6..74
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   NON_TER         83
FT                   /evidence="ECO:0000313|EMBL:EEJ52077.1"
SQ   SEQUENCE   83 AA;  9304 MW;  192401B266AEE7C5 CRC64;
     MKPIAILGGS FNPVHYGHLK MAEAAMESTH FSKVLFIPTG TPYHKEQKDL LPFADRLKLL
     ELAIEKYPDF DCSPIEGERD GNS
//
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