GenomeNet

Database: UniProt
Entry: A0A158M644_9BORD
LinkDB: A0A158M644_9BORD
Original site: A0A158M644_9BORD 
ID   A0A158M644_9BORD        Unreviewed;       197 AA.
AC   A0A158M644;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   08-MAY-2019, entry version 16.
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:KAK95351.1};
GN   ORFNames=L497_1718 {ECO:0000313|EMBL:KAK95351.1};
OS   Bordetella holmesii CDC-H585-BH.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1331206 {ECO:0000313|EMBL:KAK95351.1, ECO:0000313|Proteomes:UP000026682};
RN   [1] {ECO:0000313|EMBL:KAK95351.1, ECO:0000313|Proteomes:UP000026682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC-H585-BH {ECO:0000313|EMBL:KAK95351.1,
RC   ECO:0000313|Proteomes:UP000026682};
RA   Harvill E., Goodfield L.L., Ivanov Y., Meyer J.A., Newth C.,
RA   Cassiday P., Tondella M.L., Liao P., Zimmerman J., Meert K.,
RA   Wessel D., Berger J., Dean J.M., Holubkov R., Burr J., Liu T.,
RA   Brinkac L.M., Sanka R., Kim M., Losada L.;
RT   "Genome sequence of Bordetella holmseii.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KAK95351.1}.
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; JFZZ01000059; KAK95351.1; -; Genomic_DNA.
DR   RefSeq; WP_005014741.1; NZ_JFZZ01000059.1.
DR   EnsemblBacteria; KAK95351; KAK95351; L497_1718.
DR   PATRIC; fig|1331206.3.peg.1596; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000026682; 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; -; 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:UP000026682};
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:KAK95351.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:KAK95351.1}.
FT   DOMAIN        6    169       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   197 AA;  20875 MW;  908C81AFEBB7A6B4 CRC64;
     MKQIGLLGGS FDPIHLAHLA LAQSAMAHLG LHEVQFIPAA NPWQRAPLLA SPADRLAMIK
     AAIAGQPGLA VNSTEIDRGG ATYTVDTVRA LPAAATFTWI LGADQLANFC TWRDWQEIVR
     RVDLAVATRP GTPLQAPDAL AVLLAQQGKS LRELPFTPMA ISASDIRQRL ASGQSTAGLL
     PAAVSRYIAE HGLYLAA
//
DBGET integrated database retrieval system