ID A0A2D0KS86_9GAMM Unreviewed; 408 AA.
AC A0A2D0KS86;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Trifunctional adenylyltransferase/ribosylnicotinamide kinase/transcriptional regulator {ECO:0000313|EMBL:PHM66292.1};
GN ORFNames=Xsto_01224 {ECO:0000313|EMBL:PHM66292.1};
OS Xenorhabdus stockiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM66292.1, ECO:0000313|Proteomes:UP000222366};
RN [1] {ECO:0000313|EMBL:PHM66292.1, ECO:0000313|Proteomes:UP000222366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM66292.1,
RC ECO:0000313|Proteomes:UP000222366};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
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:PHM66292.1}.
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DR EMBL; NJAJ01000009; PHM66292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D0KS86; -.
DR Proteomes; UP000222366; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 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; 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; PF01467; CTP_transf_like; 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 Kinase {ECO:0000313|EMBL:PHM66292.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004776-1};
KW Nucleotidyltransferase {ECO:0000313|EMBL:PHM66292.1};
KW Transferase {ECO:0000313|EMBL:PHM66292.1}.
FT DOMAIN 7..56
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 408 AA; 47103 MW; 40BFAA89173EE0A8 CRC64;
MGQFDYLKEA IKQANHTLQQ VADASGMTKG YLSQLINGKI KSPSAQKLAS LHQHLGLAYP
MEKKTIGVVF GKFYPLHTGH IYLIQRASSQ VDELHVFLCY DELRDRELFI NSSMSQQPTV
SDRLRWLLQT FKYQKNIHIH SFDEQGIEPY PNGWEKWSQS AKQFMSAKGI TPQYIYSSEA
QDVPLYKEHF GIETILVDPQ RSFMNISGSQ IRQAPFRYWE YIPTEVKPFF VRTVAILGGE
SSGKSTLVNK LANMFNTTSA WEYGREYVFS HLGGDEMALQ YSDYDKIALG HAQYIDFCVK
YANKVAFIDT DFVTTQAFCK RYEGKEHPFV QALIDEYRFD LVILLENNTP WIADGLRSLG
SEQDRKAFQQ LLESMLKKNN IDYVCVNSPD YDQRFLQCVE LVQEMLAY
//
