Tag | Content |
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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 |
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59 | GVMRIPEKHLAREIE | acetylation | [1] | 185 | ALDAAGFKDTAIMSY | acetylation | [1] | 195 | AIMSYSTKFASSFYG | acetylation | [1] | 217 | SALKGDRKSYQMNPM | acetylation | [2] | 247 | GADCLMVKPAGAYLD | acetylation | [1] | 292 | AGAIDEEKVVLESLG | acetylation | [1] |
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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. |
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