| Tag | Content |
|---|
| CPLM ID | CPLM-005008 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Pyridoxal phosphate phosphatase YbhA |
Protein Synonyms/Alias | |
Gene Name | ybhA |
Gene Synonyms/Alias | b0766; JW0749 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 18 | DGTLLTPKKTLLPSS | 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 the dephosphorylation of pyridoxal-phosphate (PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and fructose-1,6-bis-phosphate (Fru1,6bisP). |
Sequence Annotation | REGION 9 11 Substrate (By similarity).
ACT_SITE 9 9 Nucleophile (By similarity).
METAL 9 9 Magnesium (By similarity).
METAL 11 11 Magnesium (By similarity).
METAL 223 223 Magnesium (By similarity). |
Keyword | Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 272 AA |
Protein Sequence | MTTRVIALDL DGTLLTPKKT LLPSSIEALA RAREAGYQLI IVTGRHHVAI HPFYQALALD 60
TPAICCNGTY LYDYHAKTVL EADPMPVIKA LQLIEMLNEH HIHGLMYVDD AMVYEHPTGH 120
VIRTSNWAQT LPPEQRPTFT QVASLAETAQ QVNAVWKFAL THDDLPQLQH FGKHVEHELG 180
LECEWSWHDQ VDIARGGNSK GKRLTKWVEA QGWSMENVVA FGDNFNDISM LEAAGTGVAM 240
GNADDAVKAR ANIVIGDNTT DSIAQFIYSH LI 272 |
Gene Ontology | GO:0000287; F:magnesium ion binding; IDA:EcoliWiki. GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:EcoliWiki. GO:0033883; F:pyridoxal phosphatase activity; IDA:EcoliWiki. GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |