CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003323
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate ammonia-lyase 
Protein Synonyms/Alias
 Aspartase 
Gene Name
 aspA 
Gene Synonyms/Alias
 b4139; JW4099 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
63KAAAMANKELQTIPKacetylation[1, 2]
70KELQTIPKSVANAIIacetylation[1, 2]
140NPNDHVNKCQSTNDAacetylation[2]
212RAFSILLKEEVKNIQacetylation[1, 2]
216ILLKEEVKNIQRTAEacetylation[1]
342VVNQVCFKVIGNDTTacetylation[1]
436KICAETGKSVREVVLacetylation[1]
Reference
 [1] 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]
 [2] 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
  
Sequence Annotation
 REGION 143 145 Substrate binding (By similarity).
 BINDING 104 104 Substrate (By similarity).  
Keyword
 3D-structure; Complete proteome; Lyase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 478 AA 
Protein Sequence
MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG MVMVKKAAAM 60
ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG GAGTSVNMNT NEVLANIGLE 120
LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT GFRIAVYSSL IKLVDAINQL REGFERKAVE 180
FQDILKMGRT QLQDAVPMTL GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN 240
TPKEYSPLAV KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL 300
LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV TMAAEAGQLQ 360
LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV CEGYVYNSIG IVTYLNPFIG 420
HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVQ NLMHPAYKAK RYTDESEQ 478 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0008797; F:aspartate ammonia-lyase activity; IDA:EcoCyc.
 GO:0006531; P:aspartate metabolic process; IDA:EcoCyc.
 GO:0008652; P:cellular amino acid biosynthetic process; IDA:EcoCyc.
 GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 
Interpro
 IPR004708; ApsA.
 IPR003031; D_crystallin.
 IPR024083; Fumarase/histidase_N.
 IPR018951; Fumarase_C_C.
 IPR000362; Fumarate_lyase.
 IPR020557; Fumarate_lyase_CS.
 IPR022761; Fumarate_lyase_N.
 IPR008948; L-Aspartase-like. 
Pfam
 PF10415; FumaraseC_C
 PF00206; Lyase_1 
SMART
  
PROSITE
 PS00163; FUMARATE_LYASES 
PRINTS
 PR00145; ARGSUCLYASE.
 PR00149; FUMRATELYASE.