| Tag | Content |
|---|
| CPLM ID | CPLM-003176 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Citrate lyase subunit beta |
Protein Synonyms/Alias | Citrase beta chain; Citrate (pro-3S)-lyase subunit beta; Citryl-CoA lyase subunit |
Gene Name | citE |
Gene Synonyms/Alias | ybdW; b0616; JW0608 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 116 | QDVLDIEKEILRIEK | 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 | Represents a citryl-ACP lyase (By similarity). |
Sequence Annotation | METAL 139 139 Magnesium (By similarity).
METAL 166 166 Magnesium (By similarity).
BINDING 76 76 Substrate (By similarity).
BINDING 139 139 Substrate (By similarity). |
Keyword | Complete proteome; Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 302 AA |
Protein Sequence | MISASLQQRK TRTRRSMLFV PGANAAMVSN SFIYPADALM FDLEDSVALR EKDTARRMVY 60
HALQHPLYRD IETIVRVNAL DSEWGVNDLE AVVRGGADVV RLPKTDTAQD VLDIEKEILR 120
IEKACGREPG STGLLAAIES PLGITRAVEI AHASERLIGI ALGAEDYVRN LRTERSPEGT 180
ELLFARCSIL QAARSAGIQA FDTVYSDANN EAGFLQEAAH IKQLGFDGKS LINPRQIDLL 240
HNLYAPTQKE VDHARRVVEA AEAAAREGLG VVSLNGKMVD GPVIDRARLV LSRAELSGIR 300
EE 302 |
Gene Ontology | GO:0009346; C:citrate lyase complex; IEA:InterPro. GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:EC. GO:0008816; F:citryl-CoA lyase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |