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UniProtKB - A1AIG7 (NUDC_ECOK1)
Protein
NAD-capped RNA hydrolase NudC
Gene
nudC
Organism
Escherichia coli O1:K1 / APEC
Status
Functioni
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
UniRule annotationCatalytic activityi
- a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + β-nicotinamide D-ribonucleotide + 2 H+UniRule annotationThis reaction proceeds in the forwardUniRule annotation direction.
- EC:3.6.1.22UniRule annotation
- EC:3.6.1.22UniRule annotation
Cofactori
Protein has several cofactor binding sites:- Mg2+UniRule annotation, Mn2+UniRule annotationNote: Divalent metal cations. Mg2+ or Mn2+.UniRule annotation
- Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 25 | SubstrateUniRule annotation | 1 | |
Binding sitei | 69 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 98 | ZincUniRule annotation | 1 | |
Metal bindingi | 101 | ZincUniRule annotation | 1 | |
Binding sitei | 111 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 116 | ZincUniRule annotation | 1 | |
Metal bindingi | 119 | ZincUniRule annotation | 1 | |
Binding sitei | 124 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 158 | Divalent metal cation 1; via carbonyl oxygenUniRule annotation | 1 | |
Metal bindingi | 174 | Divalent metal cation 2UniRule annotation | 1 | |
Metal bindingi | 174 | Divalent metal cation 3UniRule annotation | 1 | |
Metal bindingi | 178 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 178 | Divalent metal cation 3UniRule annotation | 1 | |
Metal bindingi | 219 | Divalent metal cation 1UniRule annotation | 1 | |
Metal bindingi | 219 | Divalent metal cation 3UniRule annotation | 1 | |
Binding sitei | 241 | Substrate; via amide nitrogenUniRule annotation | 1 |
GO - Molecular functioni
- magnesium ion binding Source: UniProtKB-UniRule
- manganese ion binding Source: UniProtKB-UniRule
- NAD+ diphosphatase activity Source: UniProtKB-UniRule
- RNA NAD-cap (NMN-forming) hydrolase activity Source: RHEA
- zinc ion binding Source: UniProtKB-UniRule
Keywordsi
Molecular function | Hydrolase |
Ligand | Magnesium, Manganese, Metal-binding, NAD, Zinc |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:nudCUniRule annotation Ordered Locus Names:Ecok1_39630 ORF Names:APECO1_2479 |
Organismi | Escherichia coli O1:K1 / APEC |
Taxonomic identifieri | 405955 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_1000021904 | 1 – 257 | NAD-capped RNA hydrolase NudCAdd BLAST | 257 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotationFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 125 – 248 | Nudix hydrolaseUniRule annotationAdd BLAST | 124 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 192 – 199 | Substrate bindingUniRule annotation | 8 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 159 – 180 | Nudix boxUniRule annotationAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | CLU_037162_0_1_6 |
OMAi | TWAREHR |
Family and domain databases
HAMAPi | MF_00297, Nudix_NudC, 1 hit |
InterProi | View protein in InterPro IPR022925, NADH_pyroPase_NudC IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom IPR015376, Znr_NADH_PPase |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit PF09297, zf-NADH-PPase, 1 hit |
SUPFAMi | SSF55811, SSF55811, 2 hits |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
i Sequence
Sequence statusi: Complete.
A1AIG7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDRIIEKLDH GWWVVSHEQK LWLPKGELPY GEAANFDLVG QRALQIGEWQ
60 70 80 90 100
GEPVWLVQLQ RRHDMGSVRQ VIDLDVGLFQ LAGRGVQLAE FYRSHKYCGY
110 120 130 140 150
CGHEMYPSKT EWAMLCSHCR ERYYPQIAPC IIVAIRRDDS ILLAQHTRHR
160 170 180 190 200
NGVHTVLAGF VEVGETLEQA VAREVMEESG IKVKNLRYVT SQPWPFPQSL
210 220 230 240 250
MTAFMAEYDS GEIVIDPKEL LEAHWYRYDD LPLLPPPGTV ARRLIEDTVA
MCRAEYE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000468 Genomic DNA Translation: ABJ03457.1 |
RefSeqi | WP_000373935.1, NC_008563.1 |
Genome annotation databases
EnsemblBacteriai | ABJ03457; ABJ03457; APECO1_2479 |
KEGGi | ecv:APECO1_2479 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | CP000468 Genomic DNA Translation: ABJ03457.1 |
RefSeqi | WP_000373935.1, NC_008563.1 |
3D structure databases
AlphaFoldDBi | A1AIG7 |
SMRi | A1AIG7 |
ModBasei | Search... |
Genome annotation databases
EnsemblBacteriai | ABJ03457; ABJ03457; APECO1_2479 |
KEGGi | ecv:APECO1_2479 |
Phylogenomic databases
HOGENOMi | CLU_037162_0_1_6 |
OMAi | TWAREHR |
Family and domain databases
HAMAPi | MF_00297, Nudix_NudC, 1 hit |
InterProi | View protein in InterPro IPR022925, NADH_pyroPase_NudC IPR015797, NUDIX_hydrolase-like_dom_sf IPR020084, NUDIX_hydrolase_CS IPR000086, NUDIX_hydrolase_dom IPR015376, Znr_NADH_PPase |
Pfami | View protein in Pfam PF00293, NUDIX, 1 hit PF09297, zf-NADH-PPase, 1 hit |
SUPFAMi | SSF55811, SSF55811, 2 hits |
PROSITEi | View protein in PROSITE PS51462, NUDIX, 1 hit PS00893, NUDIX_BOX, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | NUDC_ECOK1 | |
Accessioni | A1AIG7Primary (citable) accession number: A1AIG7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 15, 2008 |
Last sequence update: | January 23, 2007 | |
Last modified: | May 25, 2022 | |
This is version 80 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |