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Database: UniProt
Entry: NADD_TROWT
LinkDB: NADD_TROWT
Original site: NADD_TROWT 
ID   NADD_TROWT              Reviewed;         186 AA.
AC   Q83G58;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE            EC=2.7.7.18 {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE            Short=NaMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
GN   Name=nadD {ECO:0000255|HAMAP-Rule:MF_00244};
GN   OrderedLocusNames=TWT_469;
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=203267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist;
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide
CC       (NaAD). {ECO:0000255|HAMAP-Rule:MF_00244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-
CC         NAD(+) + 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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00244};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
CC       NAD(+) from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00244}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00244}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO44566.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE014184; AAO44566.1; ALT_INIT; Genomic_DNA.
DR   SMR; Q83G58; -.
DR   STRING; 203267.TWT_469; -.
DR   EnsemblBacteria; AAO44566; AAO44566; TWT_469.
DR   KEGG; twh:TWT_469; -.
DR   eggNOG; ENOG4108Z1W; Bacteria.
DR   eggNOG; COG1057; LUCA.
DR   KO; K00969; -.
DR   OMA; DPIHLGH; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000002200; 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; -; 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   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00482; TIGR00482; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; NAD; Nucleotide-binding;
KW   Nucleotidyltransferase; Pyridine nucleotide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN         1    186       Probable nicotinate-nucleotide
FT                                adenylyltransferase.
FT                                /FTId=PRO_0000181464.
SQ   SEQUENCE   186 AA;  20907 MW;  AACF6D6CEE8F511C CRC64;
     MGGTFDPIHH GHLVVASEVA SRFCLDEVIF VPTGRPPHKK EVSDPWHRYL MAVIATASNQ
     RFSVSKIDIE RTGPTFTVDT LRELREQLPS SDLFFITGTD ALARIFSWKD ADTLWSLAHF
     VAVSRPGHEV VDIPNDRISF LEVPAMAISS SNCRERVRSG LPIWYLVPEG VVQYIAKHGL
     YRSLYG
//
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