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Database: UniProt
Entry: Q6NFW1_CORDI
LinkDB: Q6NFW1_CORDI
Original site: Q6NFW1_CORDI 
ID   Q6NFW1_CORDI            Unreviewed;       228 AA.
AC   Q6NFW1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   31-JUL-2019, entry version 103.
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   OrderedLocusNames=DIP1775 {ECO:0000313|EMBL:CAE50305.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE50305.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M., Bentley S.D., Besra G.S., Churcher C., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Moule S., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K., Thomson N.R., Unwin L., Whitehead S.,
RA   Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium
RT   diphtheriae NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide
CC       (NaAD). {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00244, ECO:0000256|SAAS:SAAS01124450};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
CC       NAD(+) from nicotinate D-ribonucleotide: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000256|SAAS:SAAS00999967}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00244}.
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DR   EMBL; BX248359; CAE50305.1; -; Genomic_DNA.
DR   RefSeq; WP_010935326.1; NC_002935.2.
DR   EnsemblBacteria; CAE50305; CAE50305; DIP1775.
DR   KEGG; cdi:DIP1775; -.
DR   HOGENOM; HOG000262779; -.
DR   KO; K00969; -.
DR   OMA; DPIHLGH; -.
DR   OrthoDB; 1433958at2; -.
DR   BioCyc; CDIP257309:G1GT3-1800-MONOMER; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000002198; 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 {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459924};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002198};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00244, ECO:0000256|SAAS:SAAS00459916};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459927};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459933, ECO:0000313|EMBL:CAE50305.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:CAE50305.1}.
FT   DOMAIN       12    175       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   REGION      205    228       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   228 AA;  25539 MW;  48F040078F9C32FA CRC64;
     MTLPRQPSRI GIMGGTFDPI HHGHLVAASE VAARFDLELV VFVPTGQPWQ KVDREVSPAE
     DRYLMTVIAT ASNPRFTVSR VDIDRPGATY TIDTLRDLRC AYPDSELFFI TGADALGRIL
     TWRDWEKALE IATFVGVTRP GYVLEEDMLP AQYHDRVELI EIPAMAISST GCRRRAKEGL
     PVWYLVPDGV VQYIAKRQLY HPSGVDEKRN PAGAAASRLA FDRDNVEQ
//
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