| Tag | Content |
|---|
| CPLM ID | CPLM-007143 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribonucleoside-diphosphate reductase 2 subunit alpha |
Protein Synonyms/Alias | R1E protein; Ribonucleotide reductase 2 |
Gene Name | nrdE |
Gene Synonyms/Alias | b2675; JW2650 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 320 | DVERVYGKPFADVAI | 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 | Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. |
Sequence Annotation | REGION 177 178 Substrate binding (By similarity).
REGION 386 390 Substrate binding (By similarity).
REGION 588 592 Substrate binding (By similarity).
ACT_SITE 386 386 Proton acceptor (By similarity).
ACT_SITE 388 388 Cysteine radical intermediate (By
ACT_SITE 390 390 Proton acceptor (By similarity).
BINDING 161 161 Substrate (By similarity).
BINDING 206 206 Substrate; via amide nitrogen (By
DISULFID 178 415 Redox-active (By similarity). |
Keyword | Allosteric enzyme; ATP-binding; Complete proteome; Disulfide bond; DNA replication; Nucleotide-binding; Oxidoreductase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 714 AA |
Protein Sequence | MATTTAECLT QETMDYHALN AMLNLYDSAG RIQFDKDRQA VDAFIATHVR PNSVTFSSQQ 60
QRLNWLVNEG YYDESVLNRY SRDFVITLFT HAHTSGFRFQ TFLGAWKFYT SYTLKTFDGK 120
RYLEDFADRV TMVALTLAQG DETLALQLTD EMLSGRFQPA TPTFLNCGKQ QRGELVSCFL 180
LRIEDNMESI GRAVNSALQL SKRGGGVAFL LSNLREAGAP IKRIENQSSG VIPVMKMLED 240
AFSYANQLGA RQGAGAVYLH AHHPDILRFL DTKRENADEK IRIKTLSLGV VIPDITFHLA 300
KENAQMALFS PYDVERVYGK PFADVAISQH YDELVADERI RKKYLNARDF FQRLAEIQFE 360
SGYPYIMYED TVNRANPIAG RINMSNLCSE ILQVNSASEY DENLDYTRTG HDISCNLGSL 420
NIAHTMDSPD FARTVETAVR GLTAVSDMSH IRSVPSIEAG NAASHAIGLG QMNLHGYLAR 480
EGIAYGSPEA LDFTNLYFYA ITWHALRTSM LLARERGETF AGFKQSRYAS GEYFSQYLQG 540
NWQPKTAKVG ELFTRSGITL PTREMWAQLR DDVMRYGIYN QNLQAVPPTG SISYINHATS 600
SIHPIVAKVE IRKEGKTGRV YYPAPFMTNE NLALYQDAYE IGAEKIIDTY AEATRHVDQG 660
LSLTLFFPDT ATTRDINKAQ IYAWRKGIKT LYYIRLRQMA LEGTEIEGCV SCAL 714 |
Gene Ontology | GO:0005971; C:ribonucleoside-diphosphate reductase complex; IGI:EcoliWiki. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:EC. GO:0009263; P:deoxyribonucleotide biosynthetic process; IGI:EcoliWiki. GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. GO:0015949; P:nucleobase-containing small molecule interconversion; IGI:EcoliWiki. |
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