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Entry: A0A0X1SZ79_PSEAA
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ID   A0A0X1SZ79_PSEAA        Unreviewed;       229 AA.
AC   A0A0X1SZ79;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   08-MAY-2019, entry version 14.
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=AWM79_07300 {ECO:0000313|EMBL:AMB85124.1};
OS   Pseudomonas agarici.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB85124.1, ECO:0000313|Proteomes:UP000063229};
RN   [1] {ECO:0000313|EMBL:AMB85124.1, ECO:0000313|Proteomes:UP000063229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB85124.1,
RC   ECO:0000313|Proteomes:UP000063229};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; CP014135; AMB85124.1; -; Genomic_DNA.
DR   RefSeq; WP_017131409.1; NZ_FOAR01000006.1.
DR   EnsemblBacteria; AMB85124; AMB85124; AWM79_07300.
DR   OMA; DPIHLGH; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000063229; 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:UP000063229};
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:AMB85124.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00086506};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063229};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00244,
KW   ECO:0000256|SAAS:SAAS00459928, ECO:0000313|EMBL:AMB85124.1}.
FT   DOMAIN       23    199       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
SQ   SEQUENCE   229 AA;  25212 MW;  D52EE6252F9CFF33 CRC64;
     MVDKRQSAVV SGREVSPRRI GVLGGTFDPV HIGHLRSALE VVELMALDEL RLTPSARPPH
     RDTPQVSALD RLAMVDCAVA GVSPLVVDDR ELQRDKPSYT IDTLELMRAE LAAEDQLFLL
     LGWDAFCGLP TWHRWEELLQ HCHILVLQRP DADSEPPDAL RNLLAARSVS DPKALPGPGG
     HITFVWQTPL AVSATQIRQL LASGKSVRYL VPDAVLAYID AHGLYRASN
//
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