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Database: UniProt
Entry: G5SKW2_SALET
LinkDB: G5SKW2_SALET
Original site: G5SKW2_SALET 
ID   G5SKW2_SALET            Unreviewed;       410 AA.
AC   G5SKW2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Nicotinamide-nucleotide adenylyltransferase NadR {ECO:0000313|EMBL:EHC96960.1};
GN   ORFNames=LTSEWAN_6484 {ECO:0000313|EMBL:EHC96960.1};
OS   Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913086 {ECO:0000313|EMBL:EHC96960.1, ECO:0000313|Proteomes:UP000003536};
RN   [1] {ECO:0000313|EMBL:EHC96960.1, ECO:0000313|Proteomes:UP000003536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-580 {ECO:0000313|EMBL:EHC96960.1,
RC   ECO:0000313|Proteomes:UP000003536};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC96960.1}.
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DR   EMBL; AFCX01002105; EHC96960.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5SKW2; -.
DR   SMR; G5SKW2; -.
DR   PATRIC; fig|913086.3.peg.5040; -.
DR   Proteomes; UP000003536; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0050262; F:ribosylnicotinamide kinase activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   CDD; cd00093; HTH_XRE; 1.
DR   CDD; cd02019; NK; 1.
DR   CDD; cd02167; NMNAT_NadR; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR016429; NAD_NadR.
DR   InterPro; IPR038727; NadR/Ttd14_AAA_dom.
DR   InterPro; IPR006417; NadR_NMN_Atrans.
DR   InterPro; IPR041749; NMNAT_NadR.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR01526; nadR_NMN_Atrans; 1.
DR   PANTHER; PTHR37512:SF1; AAA_28 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR37512; TRIFUNCTIONAL NAD BIOSYNTHESIS/REGULATOR PROTEIN NADR; 1.
DR   Pfam; PF13521; AAA_28; 1.
DR   Pfam; PF01381; HTH_3; 1.
DR   PIRSF; PIRSF004776; NadR_NMNAT/RNK; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004776-1};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:EHC96960.1};
KW   Transferase {ECO:0000313|EMBL:EHC96960.1}.
FT   DOMAIN          7..62
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   BINDING         70..73
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT   BINDING         77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT   BINDING         144..157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT   BINDING         177..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT   BINDING         204..206
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
FT   BINDING         259..261
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004776-1"
SQ   SEQUENCE   410 AA;  47101 MW;  E06B5EFE0E6101C2 CRC64;
     MSSFDYLKTA IKQQGCTLQQ VADASGMTKG YLSQLLNAKI KSPSAQKLEA LHRFLGLEFP
     RRQKNIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGY DDTRDRGLFE DSAMSQQPTV
     SDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSNG IKAFMAEKGI QPSWIYTSEE
     ADAPQYLEHL GIETVLVDPE RTFMNISGAQ IRENPFRYWE YIPTEVKPFF VRTVAILGGE
     SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEMALQ YSDYDKIALG HAQYIDFAVK
     YANKVAFIDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
     SSVDRKAFQN LLVEMLKENN IEFVHVKEAD YDGRFLRCVE LVKEMMGEQG
//
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