Tag | Content |
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CPLM ID | CPLM-001836 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | D-serine dehydratase |
Protein Synonyms/Alias | D-serine deaminase; DSD |
Gene Name | dsdA |
Gene Synonyms/Alias | b2366; JW2363 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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17 | IAQYPLVKDLVALKE | acetylation | [1] | 93 | AMQKRLEKEYQQPIS | acetylation | [1] | 440 | EMNQYLAKGR***** | 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 | MOD_RES 118 118 N6-(pyridoxal phosphate)lysine. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 442 AA |
Protein Sequence | MENAKMNSLI AQYPLVKDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ DAHARLSRFA 60 PYLAKAFPET AATGGIIESE LVAIPAMQKR LEKEYQQPIS GQLLLKKDSH LPISGSIKAR 120 GGIYEVLAHA EKLALEAGLL TLDDDYSKLL SPEFKQFFSQ YSIAVGSTGN LGLSIGIMSA 180 RIGFKVTVHM SADARAWKKA KLRSHGVTVV EYEQDYGVAV EEGRKAAQSD PNCFFIDDEN 240 SRTLFLGYSV AGQRLKAQFA QQGRIVDADN PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH 300 CFFAEPTHSP CMLLGVHTGL HDQISVQDIG IDNLTAADGL AVGRASGFVG RAMERLLDGF 360 YTLSDQTMYD MLGWLAQEEG IRLEPSALAG MAGPQRVCAS VSYQQMHGFS AEQLRNTTHL 420 VWATGGGMVP EEEMNQYLAK GR 442 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoliWiki. GO:0008721; F:D-serine ammonia-lyase activity; IDA:EcoCyc. GO:0016836; F:hydro-lyase activity; IDA:EcoliWiki. GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc. GO:0036088; P:D-serine catabolic process; IDA:EcoCyc. GO:0051410; P:detoxification of nitrogen compound; IMP:EcoCyc. GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. |
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