Tag | Content |
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CPLM ID | CPLM-004414 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | L-serine dehydratase 1 |
Protein Synonyms/Alias | SDH 1; L-serine deaminase 1; L-SD1 |
Gene Name | sdaA |
Gene Synonyms/Alias | b1814; JW1803 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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36 | FVDDLVEKGLLDSVT | acetylation | [1] | 402 | RNAIASVKAINAARM | acetylation | [1] | 423 | APRVSLDKVIETMYE | 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 | Deaminates also threonine, particularly when it is present in high concentration. |
Sequence Annotation | |
Keyword | 4Fe-4S; Complete proteome; Direct protein sequencing; Gluconeogenesis; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 454 AA |
Protein Sequence | MISLFDMFKV GIGPSSSHTV GPMKAGKQFV DDLVEKGLLD SVTRVAVDVY GSLSLTGKGH 60 HTDIAIIMGL AGNEPATVDI DSIPGFIRDV EERERLLLAQ GRHEVDFPRD NGMRFHNGNL 120 PLHENGMQIH AYNGDEVVYS KTYYSIGGGF IVDEEHFGQD AANEVSVPYP FKSATELLAY 180 CNETGYSLSG LAMQNELALH SKKEIDEYFA HVWQTMQACI DRGMNTEGVL PGPLRVPRRA 240 SALRRMLVSS DKLSNDPMNV IDWVNMFALA VNEENAAGGR VVTAPTNGAC GIVPAVLAYY 300 DHFIESVSPD IYTRYFMAAG AIGALYKMNA SISGAEVGCQ GEVGVACSMA AAGLAELLGG 360 SPEQVCVAAE IGMEHNLGLT CDPVAGQVQV PCIERNAIAS VKAINAARMA LRRTSAPRVS 420 LDKVIETMYE TGKDMNAKYR ETSRGGLAIK VQCD 454 |
Gene Ontology | GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. GO:0003941; F:L-serine ammonia-lyase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. GO:0006565; P:L-serine catabolic process; IDA:EcoCyc. |
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