ID A0A1Y2K3K9_9PROT Unreviewed; 221 AA.
AC A0A1Y2K3K9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=MAIT1_01623 {ECO:0000313|EMBL:OSM01615.1};
OS Magnetofaba australis IT-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetofaba.
OX NCBI_TaxID=1434232 {ECO:0000313|EMBL:OSM01615.1, ECO:0000313|Proteomes:UP000194003};
RN [1] {ECO:0000313|EMBL:OSM01615.1, ECO:0000313|Proteomes:UP000194003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IT-1 {ECO:0000313|EMBL:OSM01615.1,
RC ECO:0000313|Proteomes:UP000194003};
RX PubMed=27801294; DOI=10.1186/s12864-016-3064-9;
RA Araujo A.C., Morillo V., Cypriano J., Teixeira L.C., Leao P., Lyra S.,
RA Almeida L.G., Bazylinski D.A., Vasconcellos A.T., Abreu F., Lins U.;
RT "Combined genomic and structural analyses of a cultured magnetotactic
RT bacterium reveals its niche adaptation to a dynamic environment.";
RL BMC Genomics 17:726-726(2016).
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|ARBA:ARBA00009014,
CC ECO:0000256|HAMAP-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:OSM01615.1}.
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DR EMBL; LVJN01000020; OSM01615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2K3K9; -.
DR STRING; 1434232.MAIT1_01623; -.
DR OrthoDB; 5295945at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000194003; 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:OSM01615.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00244};
KW Reference proteome {ECO:0000313|Proteomes:UP000194003};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:OSM01615.1}.
FT DOMAIN 9..191
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 221 AA; 25008 MW; C9D7AAA8F11A7092 CRC64;
MIQAQRIGLM GGSFDPPHHG HLRAALEAVE ALRLDRLLFI PTGAHPFKGE SQRMPPQHRL
AMTRLAIADE PRFDVSDIEI QRAGTAYTID TLRDLSQQFP ADELILLLGA DLLGELHLWK
DWRELLEYAH LCVMNRPGYD ARPACSLASG VLLKHQAPPD GEPIPDYDDQ YFYGALTIRD
LEISSTDLRQ RLRQGRSIRY FTPEPVIAYI QEHGLYGQAT Q
//