Tag | Content |
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CPLM ID | CPLM-004925 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Sulfate adenylyltransferase subunit 2 |
Protein Synonyms/Alias | ATP-sulfurylase small subunit; Sulfate adenylate transferase; SAT |
Gene Name | cysD |
Gene Synonyms/Alias | b2752; JW2722 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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81 | EFRDRTAKAYGCELL | acetylation | [1] | 91 | GCELLVHKNPEGVAM | acetylation | [1] | 115 | AKHTDIMKTEGLKQA | acetylation | [1] | 125 | GLKQALNKYGFDAAF | acetylation | [1] | 161 | RFHRWDPKNQRPELW | acetylation | [1] | 177 | NYNGQINKGESIRVF | acetylation | [1] | 240 | LQPGEVIKKRMVRFR | acetylation | [1] | 296 | QAGSMELKKRQGYF* | acetylation | [1] |
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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 | ATP-binding; Complete proteome; Direct protein sequencing; Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 302 AA |
Protein Sequence | MDQIRLTHLR QLEAESIHII REVAAEFSNP VMLYSIGKDS SVMLHLARKA FYPGTLPFPL 60 LHVDTGWKFR EMYEFRDRTA KAYGCELLVH KNPEGVAMGI NPFVHGSAKH TDIMKTEGLK 120 QALNKYGFDA AFGGARRDEE KSRAKERIYS FRDRFHRWDP KNQRPELWHN YNGQINKGES 180 IRVFPLSNWT EQDIWQYIWL ENIDIVPLYL AAERPVLERD GMLMMIDDNR IDLQPGEVIK 240 KRMVRFRTLG CWPLTGAVES NAQTLPEIIE EMLVSTTSER QGRVIDRDQA GSMELKKRQG 300 YF 302 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IDA:EcoCyc. GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway. GO:0000103; P:sulfate assimilation; IEA:HAMAP. GO:0019419; P:sulfate reduction; IEA:InterPro. GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |