| Tag | Content |
|---|
| CPLM ID | CPLM-005754 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | o-succinylbenzoate synthase |
Protein Synonyms/Alias | OSB synthase; OSBS; 4-(2'-carboxyphenyl)-4-oxybutyric acid synthase; o-succinylbenzoic acid synthase |
Gene Name | menC |
Gene Synonyms/Alias | b2261; JW2256 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 176 | LKGQQFAKYVNPDYR | acetylation | [1] | | 235 | GVRAVVIKPTLTGSL | acetylation | [1] | | 244 | TLTGSLEKVREQVQA | acetylation | [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 | Converts SHCHC to OSB. |
Sequence Annotation | ACT_SITE 133 133 Proton donor.
ACT_SITE 235 235 Proton acceptor.
METAL 161 161 Magnesium.
METAL 190 190 Magnesium.
METAL 213 213 Magnesium. |
Keyword | 3D-structure; Complete proteome; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 320 AA |
Protein Sequence | MRSAQVYRWQ IPMDAGVVLR DRRLKTRDGL YVCLREGERE GWGEISPLPG FSQETWEEAQ 60
SVLLAWVNNW LAGDCELPQM PSVAFGVSCA LAELTDTLPQ AANYRAAPLC NGDPDDLILK 120
LADMPGEKVA KVKVGLYEAV RDGMVVNLLL EAIPDLHLRL DANRAWTPLK GQQFAKYVNP 180
DYRDRIAFLE EPCKTRDDSR AFARETGIAI AWDESLREPD FAFVAEEGVR AVVIKPTLTG 240
SLEKVREQVQ AAHALGLTAV ISSSIESSLG LTQLARIAAW LTPDTIPGLD TLDLMQAQQV 300
RRWPGSTLPV VEVDALERLL 320 |
Gene Ontology | GO:0016836; F:hydro-lyase activity; IDA:EcoCyc. GO:0000287; F:magnesium ion binding; IEA:InterPro. GO:0009234; P:menaquinone biosynthetic process; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |