P9WH75

PR
Gene name
nrdE (Rv3051c, MTV012.66c)
Protein name
Ribonucleoside-diphosphate reductase subunit alpha
Names
Ribonucleotide reductase R1 subunit
Species
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
KEGG Pathway
mtu:Rv3051c
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)

1-50 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P9WH75

Entry ID Method Resolution Chain Position Source
AF-P9WH75-F1 Predicted AlphaFoldDB

No variants for P9WH75

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WH75

No associated diseases with P9WH75

4 regional properties for P9WH75

Type Name Position InterPro Accession
domain Ribonucleotide reductase large subunit, C-terminal 187 - 705 IPR000788
domain Ribonucleotide reductase, class I, alpha subunit, C-terminal 114 - 707 IPR013346
domain Ribonucleotide reductase large subunit, N-terminal 110 - 182 IPR013509
domain Ribonucleotide reductase N-terminal 27 - 108 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

2 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
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.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CDP reductase activity Catalysis of the reaction: dCDP + thioredoxin disulfide + H2O = CDP + thioredoxin.
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
MPPTVIAEPV ASGAHASYSG GPGETDYHAL NAMLNLYDAD GKIQFDKDRE AAHQYFLQHV
70 80 90 100 110 120
NQNTVFFHNQ DEKLDYLIRE NYYEREVLDQ YSRNFVKTLL DRAYAKKFRF PTFLGAFKYY
130 140 150 160 170 180
TSYTLKTFDG KRYLERFEDR VVMVALTLAA GDTALAELLV DEIIDGRFQP ATPTFLNSGK
190 200 210 220 230 240
KQRGEPVSCF LLRVEDNMES IGRSINSALQ LSKRGGGVAL LLTNIREHGA PIKNIENQSS
250 260 270 280 290 300
GVIPIMKLLE DAFSYANQLG ARQGAGAVYL HAHHPDIYRF LDTKRENADE KIRIKTLSLG
310 320 330 340 350 360
VVIPDITFEL AKRNDDMYLF SPYDVERVYG VPFADISVTE KYYEMVDDAR IRKTKIKARE
370 380 390 400 410 420
FFQTLAELQF ESGYPYIMFE DTVNRANPID GKITHSNLCS EILQVSTPSL FNEDLSYAKV
430 440 450 460 470 480
GKDISCNLGS LNIAKTMDSP DFAQTIEVAI RALTAVSDQT HIKSVPSIEQ GNNDSHAIGL
490 500 510 520 530 540
GQMNLHGYLA RERIFYGSDE GIDFTNIYFY TVLYHALRAS NRIAIERGTH FKGFERSKYA
550 560 570 580 590 600
SGEFFDKYTD QIWEPKTQKV RQLFADAGIR IPTQDDWRRL KESVQAHGIY NQNLQAVPPT
610 620 630 640 650 660
GSISYINHST SSIHPIVSKV EIRKEGKIGR VYYPAPYMTN DNLEYYEDAY EIGYEKIIDT
670 680 690 700 710 720
YAAATQHVDQ GLSLTLFFKD TATTRDVNKA QIYAWRKGIK TLYYIRLRQM ALEGTEVEGC
VSCML