Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | HIT-like protein HinT |
Protein Synonyms/Alias | |
Gene Name | hinT |
Gene Synonyms/Alias | ycfF; OrderedLocusNames=b1103, JW1089 |
Created Date | 3-June-2014 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Phosphorylation | Position | Peptide | Code | Type | References | 33 | VTAFRDISPQAPTHI | S | HTP | [1] | 38 | DISPQAPTHILIIPN | T | HTP | [1] | |
Reference | [1]Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Macek B,Gnad F,Soufi B,Kumar C,Olsen JV,Mijakovic I,Mann M Mol. Cell Proteomics 2008, Feb;7(2):299-307. [ PMID:17938405] |
Functional Description From UniProt | FUNCTION: Hydrolyzes purine nucleotide phosphoramidates, including adenosine 5'monophosphoramidate (AMP-NH2), adenosine 5'monophosphomorpholidate (AMP-morpholidate), guanosine 5'monophosphomorpholidate (GMP-morpholidate) and tryptamine 5'guanosine monophosphate (TpGd). Hydrolyzes lysyl-AMP (AMP-N- epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase and lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)). Required for growth at high salt concentrations Required for normal DadA activity and the ability to grow with D,L-alanine as carbon source |
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| 3D-structure; Completeproteome; Hydrolase; Nucleotide-binding; Referenceproteome |
Protein Sequence | MAEETIFSKI IRREIPSDIV YQDDLVTAFR DISPQAPTHI LIIPNILIPT VNDVSAEHEQ 60 ALGRMITVAA KIAEQEGIAE DGYRLIMNTN RHGGQEVYHI HMHLLGGRPL GPMLAHKGL 119 |
| GO:0043530 F:adenosine 5'-monophosphoramidase activity IDA:EcoCyc GO:0000166 F:nucleotide binding IEA:UniProtKB-KW GO:0055130 P:D-alanine catabolic process IMP:EcoCyc |
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