| Tag | Content |
|---|
| CPLM ID | CPLM-005953 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 3-mercaptopyruvate sulfurtransferase |
Protein Synonyms/Alias | MST; Rhodanese-like protein |
Gene Name | sseA |
Gene Synonyms/Alias | b2521; JW2505 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 88 | ELGVNQDKHLIVYDE | acetylation | [1] | | 115 | LRTFGVEKVSILGGG | acetylation | [1] | | 214 | LVREGELKTTDELDA | 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 | Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. |
Sequence Annotation | DOMAIN 17 135 Rhodanese 1.
DOMAIN 165 278 Rhodanese 2.
REGION 238 244 Substrate specificity (Potential).
ACT_SITE 238 238 Cysteine persulfide intermediate.
BINDING 179 179 Substrate (By similarity). |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Repeat; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 281 AA |
Protein Sequence | MSTTWFVGAD WLAEHIDDPE IQIIDARMAS PGQEDRNVAQ EYLNGHIPGA VFFDIEALSD 60
HTSPLPHMLP RPETFAVAMR ELGVNQDKHL IVYDEGNLFS APRAWWMLRT FGVEKVSILG 120
GGLAGWQRDD LLLEEGAVEL PEGEFNAAFN PEAVVKVTDV LLASHENTAQ IIDARPAARF 180
NAEVDEPRPG LRRGHIPGAL NVPWTELVRE GELKTTDELD AIFFGRGVSY DKPIIVSCGS 240
GVTAAVVLLA LATLDVPNVK LYDGAWSEWG ARADLPVEPV K 281 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IDA:EcoCyc. GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:EcoCyc. GO:0046677; P:response to antibiotic; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |