CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001774
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Maltodextrin phosphorylase 
Protein Synonyms/Alias
  
Gene Name
 malP 
Gene Synonyms/Alias
 b3417; JW5689 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
54LRAQPFAKPVANQRHacetylation[1]
154RQSFVDGKQVEAPDDacetylation[1]
233AHPFDLTKFNDGDFLacetylation[1]
251QQGINAEKLTKVLYPacetylation[1, 2]
359ALERWDVKLVKGLLPacetylation[1]
362RWDVKLVKGLLPRHMacetylation[1]
385RFKTLVEKTWPGDEKacetylation[1]
392KTWPGDEKVWAKLAVacetylation[1]
396GDEKVWAKLAVVHDKacetylation[1]
471ALAALLDKSLQKEWAacetylation[1]
475LLDKSLQKEWANDLDacetylation[1]
489DQLINLEKFADDAKFacetylation[1]
495EKFADDAKFRQQYREacetylation[1]
516VRLAEFVKVRTGIEIacetylation[1]
540IKRLHEYKRQHLNLLacetylation[1]
605NDPLVGDKLKVVFLPacetylation[1]
685GHTVEQVKAILAKGYacetylation[1]
690QVKAILAKGYDPVKWacetylation[1]
696AKGYDPVKWRKKDKVacetylation[1]
700DPVKWRKKDKVLDAVacetylation[1]
702VKWRKKDKVLDAVLKacetylation[1]
709KVLDAVLKELESGKYacetylation[1]
715LKELESGKYSDGDKHacetylation[1]
721GKYSDGDKHAFDQMLacetylation[1, 3]
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]
 [2] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
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 251 251 N6-acetyllysine.
 MOD_RES 646 646 N6-(pyridoxal phosphate)lysine.  
Keyword
 3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 797 AA 
Protein Sequence
MSQPIFNDKQ FQEALSRQWQ RYGLNSAAEM TPRQWWLAVS EALAEMLRAQ PFAKPVANQR 60
HVNYISMEFL IGRLTGNNLL NLGWYQDVQD SLKAYDINLT DLLEEEIDPA LGNGGLGRLA 120
ACFLDSMATV GQSATGYGLN YQYGLFRQSF VDGKQVEAPD DWHRSNYPWF RHNEALDVQV 180
GIGGKVTKDG RWEPEFTITG QAWDLPVVGY RNGVAQPLRL WQATHAHPFD LTKFNDGDFL 240
RAEQQGINAE KLTKVLYPND NHTAGKKLRL MQQYFQCACS VADILRRHHL AGRKLHELAD 300
YEVIQLNDTH PTIAIPELLR VLIDEHQMSW DDAWAITSKT FAYTNHTLMP EALERWDVKL 360
VKGLLPRHMQ IINEINTRFK TLVEKTWPGD EKVWAKLAVV HDKQVHMANL CVVGGFAVNG 420
VAALHSDLVV KDLFPEYHQL WPNKFHNVTN GITPRRWIKQ CNPALAALLD KSLQKEWAND 480
LDQLINLEKF ADDAKFRQQY REIKQANKVR LAEFVKVRTG IEINPQAIFD IQIKRLHEYK 540
RQHLNLLHIL ALYKEIRENP QADRVPRVFL FGAKAAPGYY LAKNIIFAIN KVADVINNDP 600
LVGDKLKVVF LPDYCVSAAE KLIPAADISE QISTAGKEAS GTGNMKLALN GALTVGTLDG 660
ANVEIAEKVG EENIFIFGHT VEQVKAILAK GYDPVKWRKK DKVLDAVLKE LESGKYSDGD 720
KHAFDQMLHS IGKQGGDPYL VMADFAAYVE AQKQVDVLYR DQEAWTRAAI LNTARCGMFS 780
SDRSIRDYQA RIWQAKR 797 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:EcoliWiki.
 GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
 GO:0031220; F:maltodextrin phosphorylase activity; IDA:EcoCyc.
 GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
 GO:0030980; P:alpha-glucan catabolic process; IDA:EcoliWiki.
 GO:0005980; P:glycogen catabolic process; IDA:EcoliWiki. 
Interpro
 IPR011833; Glycg_phsphrylas.
 IPR000811; Glyco_trans_35. 
Pfam
 PF00343; Phosphorylase 
SMART
  
PROSITE
 PS00102; PHOSPHORYLASE 
PRINTS