CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003341
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Delta-aminolevulinic acid dehydratase 
Protein Synonyms/Alias
 ALAD; ALADH; Porphobilinogen synthase 
Gene Name
 hemB 
Gene Synonyms/Alias
 ncf; b0369; JW0361 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
59GVMRIPEKHLAREIEacetylation[1]
185ALDAAGFKDTAIMSYacetylation[1]
195AIMSYSTKFASSFYGacetylation[1]
217SALKGDRKSYQMNPMacetylation[2]
247GADCLMVKPAGAYLDacetylation[1]
292AGAIDEEKVVLESLGacetylation[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]
 [2] 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
 Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. 
Sequence Annotation
 ACT_SITE 195 195 Schiff-base intermediate with substrate.
 ACT_SITE 247 247 Schiff-base intermediate with substrate.
 METAL 120 120 Zinc; catalytic.
 METAL 122 122 Zinc; catalytic.
 METAL 130 130 Zinc; catalytic.
 METAL 232 232 Magnesium.
 BINDING 205 205 Substrate 1.
 BINDING 216 216 Substrate 1.
 BINDING 273 273 Substrate 2.
 BINDING 312 312 Substrate 2.  
Keyword
 3D-structure; Allosteric enzyme; Complete proteome; Direct protein sequencing; Heme biosynthesis; Lyase; Magnesium; Metal-binding; Porphyrin biosynthesis; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 324 AA 
Protein Sequence
MTDLIQRPRR LRKSPALRAM FEETTLSLND LVLPIFVEEE IDDYKAVEAM PGVMRIPEKH 60
LAREIERIAN AGIRSVMTFG ISHHTDETGS DAWREDGLVA RMSRICKQTV PEMIVMSDTC 120
FCEYTSHGHC GVLCEHGVDN DATLENLGKQ AVVAAAAGAD FIAPSAAMDG QVQAIRQALD 180
AAGFKDTAIM SYSTKFASSF YGPFREAAGS ALKGDRKSYQ MNPMNRREAI RESLLDEAQG 240
ADCLMVKPAG AYLDIVRELR ERTELPIGAY QVSGEYAMIK FAALAGAIDE EKVVLESLGS 300
IKRAGADLIF SYFALDLAEK KILR 324 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004655; F:porphobilinogen synthase activity; IMP:EcoliWiki.
 GO:0006783; P:heme biosynthetic process; IMP:EcoliWiki.
 GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR001731; Porphobilinogen_synth. 
Pfam
 PF00490; ALAD 
SMART
 SM01004; ALAD 
PROSITE
 PS00169; D_ALA_DEHYDRATASE 
PRINTS
 PR00144; DALDHYDRTASE.