| Tag | Content |
|---|
| CPLM ID | CPLM-010240 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | N-succinylarginine dihydrolase |
Protein Synonyms/Alias | |
Gene Name | astB |
Gene Synonyms/Alias | ydjT; b1745; JW1734 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 88 | SDEQVLEKVARQAPH | acetylation | [1] | | 135 | TVANLNNKFHRSLEA | 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 hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2). |
Sequence Annotation | REGION 19 28 Substrate binding.
REGION 137 138 Substrate binding.
ACT_SITE 174 174
ACT_SITE 248 248
ACT_SITE 365 365 Nucleophile.
BINDING 110 110 Substrate.
BINDING 212 212 Substrate.
BINDING 250 250 Substrate.
BINDING 359 359 Substrate. |
Keyword | 3D-structure; Arginine metabolism; Complete proteome; Hydrolase; Reference proteome; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 447 AA |
Protein Sequence | MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK ALADAGFPQA 60
VIPPHERPFI PVLRQLGFSG SDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATIAPSADT 120
LDGKVHLTVA NLNNKFHRSL EAPVTESLLK AIFNDEEKFS VHSALPQVAL LGDEGAANHN 180
RLGGHYGEPG MQLFVYGREE GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD 240
VIDQGVFHND VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVSVSDTV 300
STYLFNSQLL SRDDGSMMLV LPQECREHAG VWGYLNELLA ADNPISELKV FDLRESMANG 360
GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR YYRDRLTAAD LADPQLLREG 420
REALDVLSQL LNLGSVYPFQ REGGGNG 447 |
Gene Ontology | GO:0009015; F:N-succinylarginine dihydrolase activity; IDA:EcoCyc. GO:0006527; P:arginine catabolic process; IMP:EcoliWiki. GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP. GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway. GO:0006950; P:response to stress; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |