ID A7ZVT2_ECO24 Unreviewed; 410 AA.
AC A7ZVT2;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000313|EMBL:ABV21153.1};
DE EC=2.7.7.1 {ECO:0000313|EMBL:ABV21153.1};
GN Name=nadR {ECO:0000313|EMBL:ABV21153.1};
GN OrderedLocusNames=EcE24377A_4989 {ECO:0000313|EMBL:ABV21153.1};
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV21153.1, ECO:0000313|Proteomes:UP000001122};
RN [1] {ECO:0000313|Proteomes:UP000001122}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122};
RX PubMed=18676672; DOI=10.1128/JB.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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DR EMBL; CP000800; ABV21153.1; -; Genomic_DNA.
DR RefSeq; WP_000093810.1; NC_009801.1.
DR AlphaFoldDB; A7ZVT2; -.
DR SMR; A7ZVT2; -.
DR GeneID; 75202928; -.
DR KEGG; ecw:EcE24377A_4989; -.
DR HOGENOM; CLU_052648_0_1_6; -.
DR Proteomes; UP000001122; Chromosome.
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 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:ABV21153.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001122};
KW Transferase {ECO:0000313|EMBL:ABV21153.1}.
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; 47318 MW; 52A78666211BE442 CRC64;
MSSFDYLKTA IKQQGCTLQQ VADASGMTKG YLSQLLNAKI KSPSAQKLEA LHRFLGLEFP
RQKKTIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGF DDTRDRALFE DSAMSQQPTV
PDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSNG IKKFMAEKGI QPDLIYTSEE
ADAPQYMEHL GIDTVLVDPK RTFMSISGAQ IRENPFRYWE YIPTEVKPFF VRTVAILGGE
SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEIALQ YSDYDKIALG HAQYIDFAVK
YANKVAFIDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
SSVDRKEFQN LLVEMLEENN IEFVRVEEDD YDSRFLRCVE LVREMMGEQR
//
