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Database: UniProt
Entry: A0A398BE68_9BACI
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ID   A0A398BE68_9BACI        Unreviewed;       230 AA.
AC   A0A398BE68;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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   ECO:0000313|EMBL:RID88262.1};
GN   ORFNames=D1953_04495 {ECO:0000313|EMBL:RID88262.1};
OS   Peribacillus asahii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=228899 {ECO:0000313|EMBL:RID88262.1, ECO:0000313|Proteomes:UP000266016};
RN   [1] {ECO:0000313|EMBL:RID88262.1, ECO:0000313|Proteomes:UP000266016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MA001 {ECO:0000313|EMBL:RID88262.1,
RC   ECO:0000313|Proteomes:UP000266016};
RA   Seuylemezian A., Vaishampayan P.;
RT   "Bacillus jemisoniae sp. nov., Bacillus chryseoplanitiae sp. nov., Bacillus
RT   resnikiae sp. nov., and Bacillus frankliniae sp. nov., isolated from Viking
RT   spacecraft and associated surfaces.";
RL   Submitted (AUG-2018) 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, 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}.
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:RID88262.1}.
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DR   EMBL; QWVS01000008; RID88262.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398BE68; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000266016; 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; 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:RID88262.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|HAMAP-Rule:MF_00244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266016};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000313|EMBL:RID88262.1}.
FT   DOMAIN          29..199
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   230 AA;  27003 MW;  208F88C38038AA8E CRC64;
     MTATKLYFEN LNPGKDVDAL FKEGARIGVY GSSFDPVTNV HLWTANTVRH RKKLDFVIFL
     PSSHKRVDKK LQTSDQHREE MVRLAIKNKQ TFLLDTYELH VLPGKQYTYY TMEYFKEIFP
     KADLFFIMGA DLLVDIAERK WRMDEQLVAN NQFIVMARNG IDMLKTISSS ALLRNYDDGR
     FQFLDKGLAM EISSTYIREE LARNGDPEFL LPDECYSYIK EHNLYREISR
//
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