| Tag | Content |
|---|
| CPLM ID | CPLM-010321 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cysteine desulfurase |
Protein Synonyms/Alias | Selenocysteine beta-lyase; SCL; Selenocysteine lyase; Selenocysteine reductase |
Gene Name | sufS |
Gene Synonyms/Alias | csdB; ynhB; b1680; JW1670 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 68 | LSAQATEKMENVRKR | acetylation | [1] | | 164 | LPTLFDEKTRLLAIT | 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 | Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo. |
Sequence Annotation | ACT_SITE 364 364 Cysteine persulfide intermediate.
MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. |
Keyword | 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 406 AA |
Protein Sequence | MIFSVDKVRA DFPVLSREVN GLPLAYLDSA ASAQKPSQVI DAEAEFYRHG YAAVHRGIHT 60
LSAQATEKME NVRKRASLFI NARSAEELVF VRGTTEGINL VANSWGNSNV RAGDNIIISQ 120
MEHHANIVPW QMLCARVGAE LRVIPLNPDG TLQLETLPTL FDEKTRLLAI THVSNVLGTE 180
NPLAEMITLA HQHGAKVLVD GAQAVMHHPV DVQALDCDFY VFSGHKLYGP TGIGILYVKE 240
ALLQEMPPWE GGGSMIATVS LSEGTTWTKA PWRFEAGTPN TGGIIGLGAA LEYVSALGLN 300
NIAEYEQNLM HYALSQLESV PDLTLYGPQN RLGVIAFNLG KHHAYDVGSF LDNYGIAVRT 360
GHHCAMPLMA YYNVPAMCRA SLAMYNTHEE VDRLVTGLQR IHRLLG 406 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0031071; F:cysteine desulfurase activity; IDA:EcoCyc. GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. GO:0009000; F:selenocysteine lyase activity; IDA:EcoCyc. GO:0006534; P:cysteine metabolic process; IEA:InterPro. GO:0016226; P:iron-sulfur cluster assembly; IDA:EcoCyc. GO:0001887; P:selenium compound metabolic process; IGI:EcoCyc. GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc. |
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Pfam | |
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PROSITE | |
PRINTS | |