| Tag | Content |
|---|
| CPLM ID | CPLM-003546 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable oxalyl-CoA decarboxylase |
Protein Synonyms/Alias | |
Gene Name | oxc |
Gene Synonyms/Alias | yfdU; b2373; JW2370 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 504 | LHHARYDKLMDAFRG | 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 | |
Sequence Annotation | |
Keyword | 3D-structure; Complete proteome; Decarboxylase; Lyase; Reference proteome; Thiamine pyrophosphate. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 564 AA |
Protein Sequence | MSDQLQMTDG MHIIVEALKQ NNIDTIYGVV GIPVTDMARH AQAEGIRYIG FRHEQSAGYA 60
AAASGFLTQK PGICLTVSAP GFLNGLTALA NATVNGFPMI MISGSSDRAI VDLQQGDYEE 120
LDQMNAAKPY AKAAFRVNQP QDLGIALARA IRVSVSGRPG GVYLDLPANV LAATMEKDEA 180
LTTIVKVENP SPALLPCPKS VTSAISLLAK AERPLIILGK GAAYSQADEQ LREFIESAQI 240
PFLPMSMAKG ILEDTHPLSA AAARSFALAN ADVVMLVGAR LNWLLAHGKK GWAADTQFIQ 300
LDIEPQEIDS NRPIAVPVVG DIASSMQGML AELKQNTFTT PLVWRDILNI HKQQNAQKMH 360
EKLSTDTQPL NYFNALSAVR DVLRENQDIY LVNEGANTLD NARNIIDMYK PRRRLDCGTW 420
GVMGIGMGYA IGASVTSGSP VVAIEGDSAF GFSGMEIETI CRYNLPVTIV IFNNGGIYRG 480
DGVDLSGAGA PSPTDLLHHA RYDKLMDAFR GVGYNVTTTD ELRHALTTGI QSRKPTIINV 540
VIDPAAGTES GHITKLNPKQ VAGN 564 |
Gene Ontology | GO:0043531; F:ADP binding; IDA:EcoCyc. GO:0000287; F:magnesium ion binding; IEA:InterPro. GO:0008949; F:oxalyl-CoA decarboxylase activity; IDA:EcoCyc. GO:0030976; F:thiamine pyrophosphate binding; IDA:EcoCyc. GO:0033611; P:oxalate catabolic process; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |