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Database: UniProt
Entry: A0A1F8RMN4_9CHLR
LinkDB: A0A1F8RMN4_9CHLR
Original site: A0A1F8RMN4_9CHLR 
ID   A0A1F8RMN4_9CHLR        Unreviewed;       167 AA.
AC   A0A1F8RMN4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=nicotinate-nucleotide adenylyltransferase {ECO:0000256|ARBA:ARBA00012389};
DE            EC=2.7.7.18 {ECO:0000256|ARBA:ARBA00012389};
GN   ORFNames=A2W34_04720 {ECO:0000313|EMBL:OGO48511.1};
OS   Chloroflexi bacterium RBG_16_64_32.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797658 {ECO:0000313|EMBL:OGO48511.1, ECO:0000313|Proteomes:UP000179752};
RN   [1] {ECO:0000313|EMBL:OGO48511.1, ECO:0000313|Proteomes:UP000179752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO48511.1}.
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DR   EMBL; MGNZ01000027; OGO48511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8RMN4; -.
DR   STRING; 1797658.A2W34_04720; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000179752; Unassembled WGS sequence.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:RHEA.
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; 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   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:OGO48511.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Transferase {ECO:0000313|EMBL:OGO48511.1}.
FT   DOMAIN          2..140
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   167 AA;  18591 MW;  17FD673D70999FDC CRC64;
     MLFIPAGQPW RKAGRGITSD EHRVAMLREA VGSEAAYEVA TLEVERAGPS YTVDTLETLR
     AEHPGAEMFF IVGEDALADL PNWVRPERIL ELAILAVARR AGRRANVVQE AMRRVPGLGE
     RVIWLTMSPV EVSATEIRER VRAGLPIGDM VPAAVETYIR ERGLYRE
//
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