| Tag | Content |
|---|
| CPLM ID | CPLM-004928 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Biosynthetic arginine decarboxylase |
Protein Synonyms/Alias | ADC |
Gene Name | speA |
Gene Synonyms/Alias | b2938; JW2905 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 34 | MSSQEASKMLRTYNI | acetylation | [1] | | 77 | VDLAQLVKTREAQGQ | acetylation | [1] | | 108 | RSINAAFKRARESYG | acetylation | [1] | | 127 | YFLVYPIKVNQHRRV | acetylation | [1] | | 175 | VIVCNGYKDREYIRL | acetylation | [1] | | 188 | RLALIGEKMGHKVYL | acetylation | [1] | | 192 | IGEKMGHKVYLVIEK | acetylation | [1] | | 232 | LASQGSGKWQSSGGE | 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 | Catalyzes the biosynthesis of agmatine from arginine (By similarity). |
Sequence Annotation | REGION 307 317 Substrate-binding (Potential).
MOD_RES 127 127 N6-(pyridoxal phosphate)lysine (By |
Keyword | 3D-structure; Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding; Periplasm; Polyamine biosynthesis; Putrescine biosynthesis; Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 658 AA |
Protein Sequence | MSDDMSMGLP SSAGEHGVLR SMQEVAMSSQ EASKMLRTYN IAWWGNNYYD VNELGHISVC 60
PDPDVPEARV DLAQLVKTRE AQGQRLPALF CFPQILQHRL RSINAAFKRA RESYGYNGDY 120
FLVYPIKVNQ HRRVIESLIH SGEPLGLEAG SKAELMAVLA HAGMTRSVIV CNGYKDREYI 180
RLALIGEKMG HKVYLVIEKM SEIAIVLDEA ERLNVVPRLG VRARLASQGS GKWQSSGGEK 240
SKFGLAATQV LQLVETLREA GRLDSLQLLH FHLGSQMANI RDIATGVRES ARFYVELHKL 300
GVNIQCFDVG GGLGVDYEGT RSQSDCSVNY GLNEYANNII WAIGDACEEN GLPHPTVITE 360
SGRAVTAHHT VLVSNIIGVE RNEYTVPTAP AEDAPRALQS MWETWQEMHE PGTRRSLREW 420
LHDSQMDLHD IHIGYSSGIF SLQERAWAEQ LYLSMCHEVQ KQLDPQNRAH RPIIDELQER 480
MADKMYVNFS LFQSMPDAWG IDQLFPVLPL EGLDQVPERR AVLLDITCDS DGAIDHYIDG 540
DGIATTMPMP EYDPENPPML GFFMVGAYQE ILGNMHNLFG DTEAVDVFVF PDGSVEVELS 600
DEGDTVADML QYVQLDPKTL LTQFRDQVKK TDLDAELQQQ FLEEFEAGLY GYTYLEDE 658 |
Gene Ontology | GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. GO:0008792; F:arginine decarboxylase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006527; P:arginine catabolic process; IDA:EcoCyc. GO:0009446; P:putrescine biosynthetic process; IDA:EcoCyc. GO:0008295; P:spermidine biosynthetic process; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |