| Tag | Content |
|---|
| CPLM ID | CPLM-005628 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Pyridoxal phosphate phosphatase YigL |
Protein Synonyms/Alias | PLP phosphatase; Sugar phosphatase |
Gene Name | yigL |
Gene Synonyms/Alias | b3826; JW5854 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 29 | PYAKETLKLLTARGI | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes Strongly the dephosphorylation of pyridoxal- phosphate (PLP) and moderately the dephosphorylation of 2- deoxyglucose 6-phosphate (2bGLU6P) and beta-glucose 6-phosphate (bGlu6P). Also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates. |
Sequence Annotation | REGION 8 10 Substrate (By similarity).
ACT_SITE 8 8 Nucleophile (By similarity).
METAL 8 8 Magnesium (By similarity).
METAL 10 10 Magnesium (By similarity).
METAL 214 214 Magnesium (By similarity). |
Keyword | Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 266 AA |
Protein Sequence | MYQVVASDLD GTLLSPDHTL SPYAKETLKL LTARGINFVF ATGRHHVDVG QIRDNLEIKS 60
YMITSNGARV HDLDGNLIFA HNLDRDIASD LFGVVNDNPD IITNVYRDDE WFMNRHRPEE 120
MRFFKEAVFQ YALYEPGLLE PEGVSKVFFT CDSHEQLLPL EQAINARWGD RVNVSFSTLT 180
CLEVMAGGVS KGHALEAVAK KLGYSLKDCI AFGDGMNDAE MLSMAGKGCI MGSAHQRLKD 240
LHPELEVIGT NADDAVPHYL RKLYLS 266 |
Gene Ontology | GO:0000287; F:magnesium ion binding; IDA:UniProtKB. GO:0033883; F:pyridoxal phosphatase activity; IDA:EcoliWiki. GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki. |
Interpro | |
Pfam | |
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PROSITE | |
PRINTS | |