CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
18TLSVEALKHSIAYKLacetylation[1]
31KLMFTIGKDPVVANKacetylation[1]
38KDPVVANKHEWLNATacetylation[1]
157RYDYGMFKQNIVNGSacetylation[1]
166NIVNGSQKESPDYWLacetylation[1]
182YGNPWEFKRHNTRYKacetylation[1]
259YFAAVEDKNHSENVSacetylation[1]
306SRHYQLHKTYDNLADacetylation[1]
314TYDNLADKIAIHLNDacetylation[1]
579IKADPDAKWVPRVNIacetylation[1]
599ASAYYMAKHIIHLINacetylation[1]
610HLINDVAKVINNDPQacetylation[1]
621NDPQIGDKLKVVFIPacetylation[1]
716KPREYYEKDEELHQVacetylation[1]
801FSSDRTIKEYADHIWacetylation[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
 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
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS