Tag | Content |
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CPLM ID | CPLM-002608 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NH(3)-dependent NAD(+) synthetase |
Protein Synonyms/Alias | General stress protein 38; GSP38; Spore outgrowth factor B; Sporulation protein OutB |
Gene Name | nadE |
Gene Synonyms/Alias | outB; BSU03130 |
Created Date | July 27, 2013 |
Organism | Bacillus subtilis (strain 168) |
NCBI Taxa ID | 224308 |
Lysine Modification | Position | Peptide | Type | References |
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195 | RQGRTLLKELGAPER | acetylation | [1] |
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Reference | [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG. Proteomics. 2013 May;13(10-11):1726-36. [ PMID: 23468065] |
Functional Description | Catalyzes a key step in NAD biosynthesis, transforming deamido-NAD into NAD by a two-step reaction. |
Sequence Annotation | NP_BIND 45 52 ATP. NP_BIND 168 178 NAD. BINDING 33 33 NAD. BINDING 79 79 ATP. BINDING 85 85 ATP. BINDING 138 138 NAD. BINDING 158 158 ATP. BINDING 209 209 ATP. BINDING 224 224 NAD. BINDING 259 259 NAD. |
Keyword | 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; NAD; Nucleotide-binding; Phosphoprotein; Reference proteome; Sporulation; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 272 AA |
Protein Sequence | MSMQEKIMRE LHVKPSIDPK QEIEDRVNFL KQYVKKTGAK GFVLGISGGQ DSTLAGRLAQ 60 LAVESIREEG GDAQFIAVRL PHGTQQDEDD AQLALKFIKP DKSWKFDIKS TVSAFSDQYQ 120 QETGDQLTDF NKGNVKARTR MIAQYAIGGQ EGLLVLGTDH AAEAVTGFFT KYGDGGADLL 180 PLTGLTKRQG RTLLKELGAP ERLYLKEPTA DLLDEKPQQS DETELGISYD EIDDYLEGKE 240 VSAKVSEALE KRYSMTEHKR QVPASMFDDW WK 272 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:HAMAP. GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. GO:0008795; F:NAD+ synthase activity; IEA:HAMAP. GO:0009435; P:NAD biosynthetic process; IEA:HAMAP. GO:0006950; P:response to stress; IEA:UniProtKB-KW. GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. |
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PRINTS | |