CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010289
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanine deaminase 
Protein Synonyms/Alias
 Guanase; Guanine aminase; Guanine aminohydrolase; GAH 
Gene Name
 guaD 
Gene Synonyms/Alias
 ygfP; b2883; JW5466 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
57FGEWENGKHQIPDTIacetylation[1]
128EMSAFFIKQLLRNGTacetylation[1]
313GSGLFNLKKAWQKKVacetylation[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 hydrolytic deamination of guanine, producing xanthine and ammonia. 
Sequence Annotation
 METAL 82 82 Zinc; via tele nitrogen (By similarity).
 METAL 84 84 Zinc; via tele nitrogen (By similarity).
 METAL 237 237 Zinc; via tele nitrogen (By similarity).
 METAL 327 327 Zinc (By similarity).
 BINDING 87 87 Substrate (By similarity).
 BINDING 209 209 Substrate (By similarity).
 BINDING 240 240 Substrate (By similarity).
 BINDING 276 276 Substrate (By similarity).  
Keyword
 Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 439 AA 
Protein Sequence
MMSGEHTLKA VRGSFIDVTR TIDNPEEIAS ALRFIEDGLL LIKQGKVEWF GEWENGKHQI 60
PDTIRVRDYR GKLIVPGFVD THIHYPQSEM VGAYGEQLLE WLNKHTFPTE RRYEDLEYAR 120
EMSAFFIKQL LRNGTTTALV FGTVHPQSVD ALFEAASHIN MRMIAGKVMM DRNAPDYLLD 180
TAESSYHQSK ELIERWHKNG RLLYAITPRF APTSSPEQMA MAQRLKEEYP DTWVHTHLCE 240
NKDEIAWVKS LYPDHDGYLD VYHQYGLTGK NCVFAHCVHL EEKEWDRLSE TKSSIAFCPT 300
SNLYLGSGLF NLKKAWQKKV KVGMGTDIGA GTTFNMLQTL NEAYKVLQLQ GYRLSAYEAF 360
YLATLGGAKS LGLDDLIGNF LPGKEADFVV MEPTATPLQQ LRYDNSVSLV DKLFVMMTLG 420
DDRSIYRTYV DGRLVYERN 439 
Gene Ontology
 GO:0018756; F:ammeline aminohydrolase activity; IMP:EcoCyc.
 GO:0008892; F:guanine deaminase activity; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0006147; P:guanine catabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006680; Amidohydro_1.
 IPR014311; Guanine_deaminase.
 IPR011059; Metal-dep_hydrolase_composite. 
Pfam
 PF01979; Amidohydro_1 
SMART
  
PROSITE
  
PRINTS