| Tag | Content |
|---|
| CPLM ID | CPLM-002643 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase |
Protein Synonyms/Alias | |
Gene Name | cpdB |
Gene Synonyms/Alias | b4213; JW4171 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 49 | YKDTATEKFGLVRTA | acetylation | [1] | | 550 | NYRAYGGKFAGTGDS | 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 | This bifunctional enzyme catalyzes two consecutive reactions during ribonucleic acid degradation. Converts a 2',3'- cyclic nucleotide to a 3'-nucleotide and then the 3'-nucleotide to the corresponding nucleoside and phosphate. |
Sequence Annotation | REGION 544 550 Substrate binding (By similarity).
METAL 31 31 Divalent metal cation 1 (By similarity).
METAL 33 33 Divalent metal cation 1 (By similarity).
METAL 76 76 Divalent metal cation 1 (By similarity).
METAL 76 76 Divalent metal cation 2 (By similarity).
METAL 116 116 Divalent metal cation 2 (By similarity).
METAL 225 225 Divalent metal cation 2 (By similarity).
METAL 257 257 Divalent metal cation 2 (By similarity).
METAL 259 259 Divalent metal cation 1 (By similarity).
BINDING 440 440 Substrate (By similarity). |
Keyword | Complete proteome; Direct protein sequencing; Hydrolase; Metal-binding; Multifunctional enzyme; Nucleotide-binding; Periplasm; Reference proteome; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 647 AA |
Protein Sequence | MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF GLVRTASLIN 60
DARNEVKNSV LVDNGDLIQG SPLADYMSAK GLKAGDIHPV YKALNTLDYT VGTLGNHEFN 120
YGLDYLKNAL AGAKFPYVNA NVIDARTKQP MFTPYLIKDT EVVDKDGKKQ TLKIGYIGVV 180
PPQIMGWDKA NLSGKVTVND ITETVRKYVP EMREKGADVV VVLAHSGLSA DPYKVMAENS 240
VYYLSEIPGV NAIMFGHAHA VFPGKDFADI EGADIAKGTL NGVPAVMPGM WGDHLGVVDL 300
QLSNDSGKWQ VTQAKAEARP IYDIANKKSL AAEDSKLVET LKADHDATRQ FVSKPIGKSA 360
DNMYSYLALV QDDPTVQVVN NAQKAYVEHY IQGDPDLAKL PVLSAAAPFK VGGRKNDPAS 420
YVEVEKGQLT FRNAADLYLY PNTLIVVKAS GKEVKEWLEC SAGQFNQIDP NSTKPQSLIN 480
WDGFRTYNFD VIDGVNYQID VTQPARYDGE CQMINANAER IKNLTFNGKP IDPNAMFLVA 540
TNNYRAYGGK FAGTGDSHIA FASPDENRSV LAAWIADESK RAGEIHPAAD NNWRLAPIAG 600
DKKLDIRFET SPSDKAAAFI KEKGQYPMNK VATDDIGFAI YQVDLSK 647 |
Gene Ontology | GO:0042597; C:periplasmic space; IDA:EcoCyc. GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IDA:EcoCyc. GO:0008254; F:3'-nucleotidase activity; IDA:EcoCyc. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. GO:0009166; P:nucleotide catabolic process; IEP:EcoCyc. GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |