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Database: UniProt
Entry: D3UIX1_HELM1
LinkDB: D3UIX1_HELM1
Original site: D3UIX1_HELM1 
ID   D3UIX1_HELM1            Unreviewed;       184 AA.
AC   D3UIX1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
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=HMU11910 {ECO:0000313|EMBL:CBG40446.1};
OS   Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 /
OS   12198) (Campylobacter mustelae).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40446.1, ECO:0000313|Proteomes:UP000001522};
RN   [1] {ECO:0000313|EMBL:CBG40446.1, ECO:0000313|Proteomes:UP000001522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC   {ECO:0000313|Proteomes:UP000001522};
RX   PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA   O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA   Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA   Bentley S.D.;
RT   "Comparative genomics and proteomics of Helicobacter mustelae, an
RT   ulcerogenic and carcinogenic gastric pathogen.";
RL   BMC Genomics 11:164-164(2010).
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, ECO:0000256|SAAS:SAAS01025576}.
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DR   EMBL; FN555004; CBG40446.1; -; Genomic_DNA.
DR   RefSeq; WP_013023515.1; NC_013949.1.
DR   STRING; 679897.HMU11910; -.
DR   EnsemblBacteria; CBG40446; CBG40446; HMU11910.
DR   KEGG; hms:HMU11910; -.
DR   eggNOG; ENOG4108Z1W; Bacteria.
DR   eggNOG; COG1057; LUCA.
DR   HOGENOM; HOG000262780; -.
DR   KO; K00969; -.
DR   OMA; AYQNPFK; -.
DR   OrthoDB; 1433958at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000001522; 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:UP000001522};
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:CBG40446.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001522};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:CBG40446.1}.
FT   DOMAIN        5    159       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   184 AA;  21623 MW;  D865C86215480588 CRC64;
     MHLVLYGGSF DPPHIAHIEI IKEVSKSIPM DLLVVMVAYH NPLKFPCIFS EKLRLKWMRK
     ICGEWDKVLV SDYEITHKIT YTIQTIEYLE DRYKPSQIDV ILGEDNFATL HQWHRVDELK
     KKVRFIMVRR EGFEFPSKVG QEICLKNITV PISSTQIRAS KGLERAWIPS LILQEVLENF
     KEQI
//
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