Ribonucleoside-diphosphate reductase subunit alpha

Names and origin

Protein names

Recommended name:
    Ribonucleoside-diphosphate reductase subunit alpha
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase R1 subunit

Gene names

Name:	nrdE
Ordered Locus Names:	Mb3077c

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

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Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides By similarity.
Catalytic activity	2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H₂O = ribonucleoside diphosphate + thioredoxin.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Tetramer of two alpha and two beta subunits By similarity.
Induction	Induced in response to the thiol oxidant diamide. Ref.2
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family.

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Ontologies

Keywords
Biological process	DNA replication
Ligand	ATP-binding Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro ribonucleoside-diphosphate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 725

725

Ribonucleoside-diphosphate reductase subunit alpha

PRO_0000187219

Sites

Active site

189

1

Hydrogen atom transfer By similarity

Active site

397

1

Proton acceptor By similarity

Active site

399

1

Proton acceptor By similarity

Active site

401

1

Proton acceptor By similarity

Active site

426

1

Hydrogen atom transfer By similarity

Active site

703

1

Electron transfer By similarity

Active site

704

1

Electron transfer By similarity

Site

196

1

Allosteric effector binding By similarity

Site

226

1

Allosteric effector binding By similarity

Site

720

1

Interacts with thioredoxin/glutaredoxin By similarity

Site

723

1

Interacts with thioredoxin/glutaredoxin By similarity

Amino acid modifications

Disulfide bond

189 ↔ 426

Redox-active By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A5W9-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 38C315D149331D55
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FASTA

725

82,441

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.
[2]	"Thiol specific oxidative stress response in Mycobacteria." Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y. FEMS Microbiol. Lett. 249:87-94(2005) [PubMed: 16006064] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION. Strain: BCG / Pasteur.

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Cross-references

Sequence databases
	BX248344 Genomic DNA. Translation: CAD96764.1. Different initiation.
RefSeq	NP_856722.1.
3D structure databases
SMR	P0A5W9. Positions 26-710.
ModBase	Search...
Genome annotation databases
GeneID	1093421.
GenomeReviews	Gene locus Mb3077c in contig BX248333_GR.
KEGG	mbo:Mb3077c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A5W9.
Enzyme and pathway databases
BRENDA	1.17.4.1. 3091.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR013554. Ribonucl_Rdtase_N. [Graphical view]
PANTHER	PTHR11573. Ribncl_red_lg_C. 1 hit.
Pfam	PF02867. Ribonuc_red_lgC. 1 hit. PF00317. Ribonuc_red_lgN. 1 hit. PF08343. RNR_N. 1 hit. [Graphical view]
PRINTS	PR01183. RIBORDTASEM1.
TIGRFAMs	TIGR02506. NrdE_NrdA. 1 hit.
PROSITE	PS00089. RIBORED_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

RIR1_MYCBO

Accession

Primary (citable) accession number: P0A5W9
Secondary accession number(s): O53296, P50640

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	July 28, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents