Tag | Content |
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CPLM ID | CPLM-003335 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glycogen phosphorylase |
Protein Synonyms/Alias | |
Gene Name | glgP |
Gene Synonyms/Alias | glgY; b3428; JW3391 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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18 | TLSVEALKHSIAYKL | acetylation | [1] | 31 | KLMFTIGKDPVVANK | acetylation | [1] | 38 | KDPVVANKHEWLNAT | acetylation | [1] | 157 | RYDYGMFKQNIVNGS | acetylation | [1] | 166 | NIVNGSQKESPDYWL | acetylation | [1] | 182 | YGNPWEFKRHNTRYK | acetylation | [1] | 259 | YFAAVEDKNHSENVS | acetylation | [1] | 306 | SRHYQLHKTYDNLAD | acetylation | [1] | 314 | TYDNLADKIAIHLND | acetylation | [1] | 579 | IKADPDAKWVPRVNI | acetylation | [1] | 599 | ASAYYMAKHIIHLIN | acetylation | [1] | 610 | HLINDVAKVINNDPQ | acetylation | [1] | 621 | NDPQIGDKLKVVFIP | acetylation | [1] | 716 | KPREYYEKDEELHQV | acetylation | [1] | 801 | FSSDRTIKEYADHIW | acetylation | [1] |
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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 | Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. |
Sequence Annotation | MOD_RES 662 662 N6-(pyridoxal phosphate)lysine (By |
Keyword | Allosteric enzyme; Carbohydrate metabolism; Complete proteome; Glycogen metabolism; Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 815 AA |
Protein Sequence | MNAPFTYSSP TLSVEALKHS IAYKLMFTIG KDPVVANKHE WLNATLFAVR DRLVERWLRS 60 NRAQLSQETR QVYYLSMEFL IGRTLSNAML SLGIYEDVQG ALEAMGLNLE ELIDEENDPG 120 LGNGGLGRLA ACFLDSLATL GLPGRGYGIR YDYGMFKQNI VNGSQKESPD YWLEYGNPWE 180 FKRHNTRYKV RFGGRIQQEG KKTRWIETEE ILGVAYDQII PGYDTDATNT LRLWSAQASS 240 EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SSTIQDILSR 300 HYQLHKTYDN LADKIAIHLN DTHPVLSIPE MMRLLIDEHQ FSWDDAFEVC CQVFSYTNHT 360 LMSEALETWP VDMLGKILPR HLQIIFEIND YFLKTLQEQY PNDTDLLGRA SIIDESNGRR 420 VRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFAKIFPGR FTNVTNGVTP RRWLAVANPS 480 LSAVLDEHLG RNWRTDLSLL NELQQHCDFP MVNHAVHQAK LENKKRLAEY IAQQLNVVVN 540 PKALFDVQIK RIHEYKRQLM NVLHVITRYN RIKADPDAKW VPRVNIFGGK AASAYYMAKH 600 IIHLINDVAK VINNDPQIGD KLKVVFIPNY SVSLAQLIIP AADLSEQISL AGTEASGTSN 660 MKFALNGALT IGTLDGANVE MLDHVGADNI FIFGNTAEEV EELRRQGYKP REYYEKDEEL 720 HQVLTQIGSG VFSPEDPGRY RDLVDSLINF GDHYQVLADY RSYVDCQDKV DELYELQEEW 780 TAKAMLNIAN MGYFSSDRTI KEYADHIWHI DPVRL 815 |
Gene Ontology | GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0016052; P:carbohydrate catabolic process; IDA:EcoliWiki. GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |