| Tag | Content |
|---|
| CPLM ID | CPLM-013222 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cysteine sulfinate desulfinase |
Protein Synonyms/Alias | CSD |
Gene Name | csdA |
Gene Synonyms/Alias | ygdJ; b2810; JW2781 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 82 | LLNAPDDKTIVWTRG | acetylation | [1] | | 314 | LAEDALAKRPGFRSF | acetylation | [1] | | 382 | SFAPYNTKSDVDALV | 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 | Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L- selenocystine to produce L-alanine. L-cysteine sulfinic acid is the best substrate. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. |
Sequence Annotation | ACT_SITE 358 358 Probable.
MOD_RES 222 222 N6-(pyridoxal phosphate)lysine (By |
Keyword | Complete proteome; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 401 AA |
Protein Sequence | MNVFNPAQFR AQFPALQDAG VYLDSAATAL KPEAVVEATQ QFYSLSAGNV HRSQFAEAQR 60
LTARYEAARE KVAQLLNAPD DKTIVWTRGT TESINMVAQC YARPRLQPGD EIIVSVAEHH 120
ANLVPWLMVA QQTGAKVVKL PLNAQRLPDV DLLPELITPR SRILALGQMS NVTGGCPDLA 180
RAITFAHSAG MVVMVDGAQG AVHFPADVQQ LDIDFYAFSG HKLYGPTGIG VLYGKSELLE 240
AMSPWLGGGK MVHEVSFDGF TTQSAPWKLE AGTPNVAGVI GLSAALEWLA DYDINQAESW 300
SRSLATLAED ALAKRPGFRS FRCQDSSLLA FDFAGVHHSD MVTLLAEYGI ALRAGQHCAQ 360
PLLAELGVTG TLRASFAPYN TKSDVDALVN AVDRALELLV D 401 |
Gene Ontology | GO:0031071; F:cysteine desulfurase activity; IEA:InterPro. GO:0016829; F:lyase activity; IEA:UniProtKB-KW. GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. GO:0016783; F:sulfurtransferase activity; IDA:EcoCyc. GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. GO:0000096; P:sulfur amino acid metabolic process; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |