P50620

PR
Gene name
nrdE
Protein name
Ribonucleoside-diphosphate reductase subunit alpha
Names
Ribonucleotide reductase large subunit
Species
Bacillus subtilis (strain 168)
KEGG Pathway
bsu:BSU17380
EC number
1.17.4.1: With a disulfide as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

291-368 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

9 structures for P50620

Entry ID Method Resolution Chain Position Source
6CGL X-ray 320 A A/B 1-700 PDB
6CGM X-ray 200 A A 1-700 PDB
6CGN X-ray 226 A A 1-700 PDB
6MT9 X-ray 250 A A 1-700 PDB
6MV9 X-ray 295 A A/B 1-700 PDB
6MVE X-ray 255 A A 1-700 PDB
6MW3 EM 465 A C/D 1-700 PDB
6MYX EM 600 A C/D/I/J 1-700 PDB
AF-P50620-F1 Predicted AlphaFoldDB

No variants for P50620

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P50620

No associated diseases with P50620

4 regional properties for P50620

Type Name Position InterPro Accession
domain Ribonucleotide reductase large subunit, C-terminal 168 - 684 IPR000788
domain Ribonucleotide reductase, class I, alpha subunit, C-terminal 95 - 688 IPR013346
domain Ribonucleotide reductase large subunit, N-terminal 91 - 163 IPR013509
domain Ribonucleotide reductase N-terminal 9 - 89 IPR013554

Functions

Description
EC Number 1.17.4.1 With a disulfide as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
ribonucleoside-diphosphate reductase complex An enzyme complex composed of 2-4 or more subunits, which usually contains nonheme iron and requires ATP for catalysis. Catalyzes the formation of 2'-deoxyribonucleoside diphosphate from ribonucleoside diphosphate, using either thioredoxin disulfide or glutaredoxin disulfide as an acceptor.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin.

2 GO annotations of biological process

Name Definition
deoxyribonucleotide biosynthetic process The chemical reactions and pathways resulting in the formation of a deoxyribonucleotide, a compound consisting of deoxyribonucleoside (a base linked to a deoxyribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSQNQVPKWI QLNNEIMIQK DGKFQFDKDK EAVHSYFVDY INQNTVFFHN LKEKLDYLVE
70 80 90 100 110 120
NQYYEEEFLS LYSFEDIKEV FKTAYAKKFR FPSFMSAFKF YNDYALKTND KKKILERYED
130 140 150 160 170 180
RISIVALFFA NGDTEKAKEY VNLMINQEYQ PSTPTFLNAG RKRRGELVSC FLLEVNDSLN
190 200 210 220 230 240
DISRAIDISM QLSKLGGGVS LNLSKLRAKG EAIKDVENAT KGVVGVMKLL DNAFRYADQM
250 260 270 280 290 300
GQRQGSGAAY LNIFHRDIND FLDTKKISAD EDVRVKTLSI GVVIPDKFVE LAREDKAAYV
310 320 330 340 350 360
FYPHTIYKEY GQHMDEMDMN EMYDKFVDNP RVKKEKINPR KLLEKLAMLR SESGYPYIMF
370 380 390 400 410 420
QDNVNKVHAN NHISKVKFSN LCSEVLQASQ VSSYTDYDEE DEIGLDISCN LGSLNILNVM
430 440 450 460 470 480
EHKSIEKTVK LATDSLTHVS ETTDIRNAPA VRRANKAMKS IGLGAMNLHG YLAQNGIAYE
490 500 510 520 530 540
SPEARDFANT FFMMVNFYSI QRSAEIAKEK GETFDQYEGS TYATGEYFDK YVSTDFSPKY
550 560 570 580 590 600
EKIANLFEGM HIPTTEDWKK LKAFVAEHGM YHSYRLCIAP TGSISYVQSS TASVMPIMER
610 620 630 640 650 660
IEERTYGNSK TYYPMPGLAS NNWFFYKEAY DMDMFKVVDM IATIQQHIDQ GISFTLFLKD
670 680 690
TMTTRDLNRI DLYAHHRGIK TIYYARTKDT GQDSCLSCVV