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Database: UniProt
Entry: A0A2P8VMN6_9ENTR
LinkDB: A0A2P8VMN6_9ENTR
Original site: A0A2P8VMN6_9ENTR 
ID   A0A2P8VMN6_9ENTR        Unreviewed;       410 AA.
AC   A0A2P8VMN6;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR {ECO:0000313|EMBL:PSN08819.1};
DE            EC=2.7.7.1 {ECO:0000313|EMBL:PSN08819.1};
GN   ORFNames=C7G83_05545 {ECO:0000313|EMBL:PSN08819.1};
OS   Siccibacter turicensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Siccibacter.
OX   NCBI_TaxID=357233 {ECO:0000313|EMBL:PSN08819.1, ECO:0000313|Proteomes:UP000240212};
RN   [1] {ECO:0000313|EMBL:PSN08819.1, ECO:0000313|Proteomes:UP000240212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6100069499-17 {ECO:0000313|EMBL:PSN08819.1,
RC   ECO:0000313|Proteomes:UP000240212};
RA   Lepuschitz S., Pekard-Amenitsch S., Haunold R., Schill S., Mach R.,
RA   Allerberger F., Ruppitsch W., Forsythe S.J.;
RT   "Draft genome sequence of the first documented clinical Siccibacter
RT   turicensis isolate in Austria.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSN08819.1}.
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DR   EMBL; PYEP01000002; PSN08819.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8VMN6; -.
DR   STRING; 1388748.GCA_000463155_03268; -.
DR   OrthoDB; 3249147at2; -.
DR   Proteomes; UP000240212; 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:UniProtKB-EC.
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   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; 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:PSN08819.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR004776-1};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:PSN08819.1};
KW   Transferase {ECO:0000313|EMBL:PSN08819.1}.
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;  47082 MW;  E4446D8BB44184DE CRC64;
     MSSFDYLKTA IRQQGCTLQQ VAAACGMTKG YLSQLLNAKI KSPSAQKLEA LHRFLGLEFP
     RKQKNIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGY DDKRDRALFD ASAMSQQPTV
     PDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSHG IKGFMEEKGI APDWIYTSEE
     ADAAQYLEHL GIETVLIDPK RTFMNISGSQ IRENPFRYWE YIPTEVKPFF VRTVAVLGGE
     SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEMALQ YSDYDKIALG HAQYIDFAVK
     YANKVAFVDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
     SSVDRTEFQS MLIDMLDANH IDYVHVKESD YDTRFLRCVD LVKKLMGEQG
//
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