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Database: UniProt
Entry: R8ANI1_PLESH
LinkDB: R8ANI1_PLESH
Original site: R8ANI1_PLESH 
ID   R8ANI1_PLESH            Unreviewed;       225 AA.
AC   R8ANI1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-MAY-2019, entry version 31.
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:EON87904.1};
GN   ORFNames=PLESHI_13318 {ECO:0000313|EMBL:EON87904.1};
OS   Plesiomonas shigelloides 302-73.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   unclassified Enterobacterales; Plesiomonas.
OX   NCBI_TaxID=1315976 {ECO:0000313|EMBL:EON87904.1, ECO:0000313|Proteomes:UP000014012};
RN   [1] {ECO:0000313|EMBL:EON87904.1, ECO:0000313|Proteomes:UP000014012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=302-73 {ECO:0000313|EMBL:EON87904.1,
RC   ECO:0000313|Proteomes:UP000014012};
RX   PubMed=23814109;
RA   Pique N., Aquilini E., Alioto T., Minana-Galbis D., Tomas J.M.;
RT   "Genome Sequence of Plesiomonas shigelloides Strain 302-73 (Serotype
RT   O1).";
RL   Genome Announc. 1:e00404-13(2013).
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:EON87904.1}.
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DR   EMBL; AQQO01000357; EON87904.1; -; Genomic_DNA.
DR   RefSeq; WP_010864268.1; NZ_KB944511.1.
DR   EnsemblBacteria; EON87904; EON87904; PLESHI_13318.
DR   PATRIC; fig|1315976.3.peg.2531; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000014012; 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; 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:UP000014012};
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:EON87904.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014012};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:EON87904.1}.
FT   DOMAIN       17    197       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   225 AA;  25361 MW;  222F09D44DBFF316 CRC64;
     MTEHALSPAA TLPLIGLYGG TFDPLHRGHL EPVQALARTL QLSQVRLMPN NVPPHRPQPV
     ASAAQRAEMV RLACAANPLF VPDLRELQRS TPSYTIETLE EVRREIGPRQ PLAFIIGQDS
     LLTLPSWFRW QELTDYAHLL VCARPGYARM PDDVAFQRWL HLRLTTDCNV LHHQPAGTVF
     LAETPEYPIS ATAIRQRLQN GQPCDDWLTC EVATYITQHG LYSSR
//
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