GenomeNet

Database: UniProt
Entry: G9WG42_9LACT
LinkDB: G9WG42_9LACT
Original site: G9WG42_9LACT 
ID   G9WG42_9LACT            Unreviewed;       217 AA.
AC   G9WG42;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-MAY-2019, entry version 41.
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=OKIT_1542 {ECO:0000313|EMBL:EHN59620.1};
OS   Oenococcus kitaharae DSM 17330.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
OC   Oenococcus.
OX   NCBI_TaxID=1045004 {ECO:0000313|EMBL:EHN59620.1, ECO:0000313|Proteomes:UP000004959};
RN   [1] {ECO:0000313|EMBL:EHN59620.1, ECO:0000313|Proteomes:UP000004959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM17330 {ECO:0000313|Proteomes:UP000004959};
RX   PubMed=22235313; DOI=10.1371/journal.pone.0029626;
RA   Borneman A.R., McCarthy J.M., Chambers P.J., Bartowsky E.J.;
RT   "Functional divergence in the genus oenococcus as predicted by genome
RT   sequencing of the newly-described species, Oenococcus kitaharae.";
RL   PLoS ONE 7:E29626-E29626(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHN59620.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AFVZ01000001; EHN59620.1; -; Genomic_DNA.
DR   RefSeq; WP_007746631.1; NZ_KE386622.1.
DR   STRING; 1045004.OKIT_1542; -.
DR   EnsemblBacteria; EHN59620; EHN59620; OKIT_1542.
DR   PATRIC; fig|1045004.4.peg.1513; -.
DR   OrthoDB; 1433958at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000004959; 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; 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:UP000004959};
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:EHN59620.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004959};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:EHN59620.1}.
FT   DOMAIN       31    187       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   217 AA;  24430 MW;  FC1125201CF2BB84 CRC64;
     MNLLTSFSSM TALSQPETSL DRLKEKHRIG IFGGTFNPIH NGQLIAAEQV CTQLGLDRVY
     FMPDAVPFGG THENAVEPST RSEMIRLAIR GNSKFDIELT PIHDGGQQST YSVLKKLTTA
     HPENDYYLIM GAHLIRQISS WDQVSSLTKL VHLVAIEEPG VARNSDFQAI WVYVNWLNIS
     SSDIRSRLRT RQSVRYLIPD VVAAYIAEYG LYQGRFL
//
DBGET integrated database retrieval system