| Tag | Content |
|---|
| CPLM ID | CPLM-004816 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glucose-1-phosphatase |
Protein Synonyms/Alias | G1Pase |
Gene Name | agp |
Gene Synonyms/Alias | b1002; JW0987 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 199 | DSPACKEKQQCSLVD | acetylation | [1] | | 214 | GKNTFSAKYQQEPGV | acetylation | [1] | | 293 | PLVSYIDKALVTDRT | 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 | Absolutely required for the growth of E.coli in a high- phosphate medium containing G-1-P as the sole carbon source. |
Sequence Annotation | REGION 311 313 Substrate binding.
ACT_SITE 40 40 Nucleophile.
ACT_SITE 312 312 Proton donor.
BINDING 39 39 Substrate.
BINDING 43 43 Substrate.
BINDING 116 116 Substrate.
BINDING 218 218 Substrate. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; Periplasm; Reference proteome; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 413 AA |
Protein Sequence | MNKTLIAAAV AGIVLLASNA QAQTVPEGYQ LQQVLMMSRH NLRAPLANNG SVLEQSTPNK 60
WPEWDVPGGQ LTTKGGVLEV YMGHYMREWL AEQGMVKSGE CPPPYTVYAY ANSLQRTVAT 120
AQFFITGAFP GCDIPVHHQE KMGTMDPTFN PVITDDSAAF SEQAVAAMEK ELSKLQLTDS 180
YQLLEKIVNY KDSPACKEKQ QCSLVDGKNT FSAKYQQEPG VSGPLKVGNS LVDAFTLQYY 240
EGFPMDQVAW GEIKSDQQWK VLSKLKNGYQ DSLFTSPEVA RNVAKPLVSY IDKALVTDRT 300
SAPKITVLVG HDSNIASLLT ALDFKPYQLH DQNERTPIGG KIVFQRWHDS KANRDLMKIE 360
YVYQSAEQLR NADALTLQAP AQRVTLELSG CPIDADGFCP MDKFDSVLNE AVK 413 |
Gene Ontology | GO:0042597; C:periplasmic space; IPI:EcoCyc. GO:0016158; F:3-phytase activity; IDA:EcoCyc. GO:0003993; F:acid phosphatase activity; IEA:InterPro. GO:0008877; F:glucose-1-phosphatase activity; IDA:EcoCyc. GO:0006006; P:glucose metabolic process; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |