| Tag | Content |
|---|
| CPLM ID | CPLM-003711 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribonucleoside-diphosphate reductase subunit alpha 1 |
Protein Synonyms/Alias | Ribonucleotide reductase R1 subunit 1 |
Gene Name | nrdE1 |
Gene Synonyms/Alias | MSMEG_1019; MSMEI_0990 |
Created Date | July 27, 2013 |
Organism | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) |
NCBI Taxa ID | 246196 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 310 | ITFELAKKNEDMYLF | pupylation | [1] |
|
Reference | [1] Expansion of the mycobacterial "PUPylome". Watrous J, Burns K, Liu WT, Patel A, Hook V, Bafna V, Barry CE 3rd, Bark S, Dorrestein PC. Mol Biosyst. 2010 Feb;6(2):376-85. [ PMID: 20094657] |
Functional Description | Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity). |
Sequence Annotation | REGION 185 186 Substrate binding (By similarity).
REGION 394 398 Substrate binding (By similarity).
REGION 596 600 Substrate binding (By similarity).
ACT_SITE 394 394 Proton acceptor (By similarity).
ACT_SITE 396 396 Cysteine radical intermediate (By
ACT_SITE 398 398 Proton acceptor (By similarity).
BINDING 169 169 Substrate (By similarity).
BINDING 214 214 Substrate; via amide nitrogen (By
DISULFID 186 423 Redox-active (By similarity).
CROSSLNK 310 310 Isoglutamyl lysine isopeptide (Lys-Gln) |
Keyword | Allosteric enzyme; ATP-binding; Complete proteome; Disulfide bond; DNA replication; Isopeptide bond; Nucleotide-binding; Oxidoreductase; Reference proteome; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 722 AA |
Protein Sequence | MPPTVTAAEP VTTTGHVLPG EADYHALNAM LNLYDADGKI QFEKDREAAK QYFLQHVNQN 60
TVFFHSQDEK LDYLIENEYY EREVLDQYSR DFIKSLLDRA YAKKFRFPTF LGAFKYYTSY 120
TLKTFDGKRY LERFEDRVVM VALTLAAGDT ELAEKLVDEI IDGRFQPATP TFLNSGKKQR 180
GEPVSCFLLR IEDNMESIGR SINSALQLSK RGGGVALLLS NIREHGAPIK NIENQSSGVI 240
PIMKLLEDSF SYANQLGARQ GAGAVYLHAH HPDIYRFLDT KRENADEKIR IKTLSLGVVI 300
PDITFELAKK NEDMYLFSPY DVERVYGVPF ADVSVTEKYY EMVDDARIRK TKINAREFFQ 360
TLAELQFESG YPYIMFEDTV NRSNPIAGKI THSNLCSEIL QVSTPSEFND DLSYAKVGKD 420
ISCNLGSLNI AKAMDSPDFA QTIEVAIRAL TAVSDQTHIT SVPSIEQGNN DSHAIGLGQM 480
NLHGYLARER IYYGSEEGID FTNIYFYTVL FHALRASNKI AIERGTHFKG FEKSKYASGE 540
FFDKYTDQVW EPKTDKVRRL FADADIHIPT QDDWKQLKES VQKHGIYNQN LQAVPPTGSI 600
SYINHSTSSI HPVASKIEIR KEGKIGRVYY PAPYMTNDNL DYYQDAYEIG YEKIIDTYAA 660
ATQHVDQGLS LTLFFKDTAT TRDVNKAQIY AWRKGIKTLY YIRLRQMALE GTEVEGCVSC 720
ML 722 |
Gene Ontology | GO:0005971; C:ribonucleoside-diphosphate reductase complex; IEA:InterPro. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:EC. GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |