Q9L646

PR
Gene name
nrdD (STM4452)
Protein name
Anaerobic ribonucleoside-triphosphate reductase
Names
Class III ribonucleoside-triphosphate reductase
Species
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
KEGG Pathway
stm:STM4452
EC number
1.1.98.6: With other, known, acceptors
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

67-151 (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 Q9L646

Entry ID Method Resolution Chain Position Source
AF-Q9L646-F1 Predicted AlphaFoldDB

No variants for Q9L646

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9L646

No associated diseases with Q9L646

3 regional properties for Q9L646

Type Name Position InterPro Accession
domain Glycine radical domain 583 - 708 IPR001150
domain ATP-cone domain 3 - 92 IPR005144
conserved_site Formate C-acetyltransferase glycine radical, conserved site 676 - 684 IPR019777

Functions

Description
EC Number 1.1.98.6 With other, known, acceptors
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
anaerobic ribonucleoside-triphosphate reductase complex An enzyme complex composed of 4 subunits, 2 copies of the large protein (nrdD in E. coli) and 2 copies of the small protein (nrdG in E. coli). It catalyzes the generation of 2'deoxyribonucleotides under anaerobic growth conditions. The larger subunit is the catalytic unit that is activated by the smaller iron-binding subunit.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
ribonucleoside-triphosphate reductase activity Catalysis of the reaction: 2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O = ribonucleoside triphosphate + thioredoxin.

2 GO annotations of biological process

Name Definition
2'-deoxyribonucleotide biosynthetic process The chemical reactions and pathways resulting in the formation of a 2'-deoxyribonucleotide, a compound consisting of 2'-deoxyribonucleoside (a base linked to a 2'-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
MTPHVMKRDG CKVPFKSERI KEAILRAAKA AGVDDADYCA TVAEVVSSQM NARSQVDINE
70 80 90 100 110 120
IQTAVENQLM SGPYKQLARA YIEYRHDRDI QREKRGRLNQ EIRGLVEQTN SALLNENANK
130 140 150 160 170 180
DSKVIPTQRD LLAGIVAKHY ARQHLLPRDV VQAHERGDIH YHDLDYSPFF PMFNCMLIDL
190 200 210 220 230 240
KGMLTQGFKM GNAEIEPPKS ISTATAVTAQ IIAQVASHIY GGTTINRIDE VLAPFVTESY
250 260 270 280 290 300
NKHRKTADEW QIPDAEGYAR SRTEKECYDA FQSLEYEVNT LHTANGQTPF VTFGFGLGTS
310 320 330 340 350 360
WESRLIQASI LRNRIAGLGK NRKTAVFPKL VFAIRDGLNH KFGDPNYDIK QLALECASKR
370 380 390 400 410 420
MYPDILNYDQ VVKVTGSFKT PMGCRSFLGV WENENGEQIH DGRNNLGVIS LNLPRIALEA
430 440 450 460 470 480
KGDETAFWKL LDERLALARK ALMTRIARLE GVKARVAPIL YMEGACGVRL KADDDVSEIF
490 500 510 520 530 540
KNGRASISLG YIGIHETINA LFGGEHLYDS EQLRAKGIAI VERLRQAVDQ WKDETGYGFS
550 560 570 580 590 600
LYSTPSENLC DRFCRLDTAE FGVVPGVTDK GYYTNSFHLD VEKKVNPYDK IDFEAPYPPL
610 620 630 640 650 660
ANGGFICYGE YPNIQHNLKA LEDVWDYSYQ HVPYYGTNTP IDECYECGFT GEFECTSKGF
670 680 690 700 710
TCPKCGNHDA ARVSVTRRVC GYLGSPDARP FNAGKQEEVK RRVKHLGNGQ IG