Reviewed, UniProtKB/Swiss-Prot Q9CBQ0 (RIR1_MYCLE)

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:	ML1734

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	721 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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.
Enzyme regulation	Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction By similarity.
Pathway	Genetic information processing; DNA replication.
Subunit structure	Tetramer of two alpha and two beta subunits By similarity.
Sequence similarities	Belongs to the ribonucleoside diphosphate reductase large chain family.

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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 721	721	Ribonucleoside-diphosphate reductase subunit alpha		PRO_0000187220
Regions
	Region	184 – 185	2	Substrate binding By similarity
	Region	393 – 397	5	Substrate binding By similarity
	Region	595 – 599	5	Substrate binding By similarity
Sites
	Active site	393	1	Proton acceptor By similarity
	Active site	395	1	Cysteine radical intermediate By similarity
	Active site	397	1	Proton acceptor By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	213	1	Substrate; via amide nitrogen By similarity
	Site	185	1	Important for hydrogen atom transfer By similarity
	Site	192	1	Allosteric effector binding By similarity
	Site	222	1	Allosteric effector binding By similarity
	Site	422	1	Important for hydrogen atom transfer By similarity
	Site	699	1	Important for electron transfer By similarity
	Site	700	1	Important for electron transfer By similarity
	Site	716	1	Interacts with thioredoxin/glutaredoxin By similarity
	Site	719	1	Interacts with thioredoxin/glutaredoxin By similarity
Amino acid modifications
	Disulfide bond	185 ↔ 422		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CBQ0-1 [UniParc]. Last modified August 29, 2001. Version 2. Checksum: 22B365A016228872	FASTA	721	82,024
	10 20 30 40 50 60 MPPTATAEPV TASTHMLSNE TDYHALNAML NLYDADGKIQ FDKDVLAARQ FFLQHVNQNT 70 80 90 100 110 120 VFFHNQDEKL DYLIRENYYE REVLDQYSRN FVKSLLDRAY AKKFRFSTFL GAFKYYTSYT 130 140 150 160 170 180 LKTFDGKRYL ERLEDRVCMV ALTLAAGDTG LAEKLVDEII DGRFQPATPT FLNSGKKQRG 190 200 210 220 230 240 EPVSCFLLRI EDNMESIGRS VNSALQLSKR GGGVALLLSN IREHGAPIKN IEHQSSGVIP 250 260 270 280 290 300 IMKLLEDAFS YANQLGARQG AGAVYLHAHH PDIYRFLDTK RENADEKIRI KTLSLGVIIP 310 320 330 340 350 360 DITFELAKRN EDMYLFSSYD VERVYEVPFA DISVTEKYYE MLDDARIRKT KIKAREFFQK 370 380 390 400 410 420 LAELQFESGY PYVMFEDTVN RANPIEGKIT HSNLCSEILQ VSTPSLFNDD LSYAKVGKDI 430 440 450 460 470 480 SCNLGSLNIA KTMDSPDFAQ TVEVAIRALT AVSDQTHIKS VPSIEQGNND SHAIGLGQMN 490 500 510 520 530 540 LHGYLSREGI FYGSEEGVDF TNIYFYTVLF HVLLASNSIA IERGTFFKGF ERSKYASGEF 550 560 570 580 590 600 FDKYIEQTWE PKTDKVRQLF AEAAIRIPTQ NDWKRLKELV VAHGIYNQNL QAVPPTGSIS 610 620 630 640 650 660 YINHSTSSIH PIVSKVEIRK EGKIGRVYYP APYMTNDNLQ YYQDAYEIGY QKIIDTYAAA 670 680 690 700 710 720 TQHVDQGLSL TLFFKDTATT RDVNKAQIYA WRKGIKTLYY IRLRQMALEG TEVEGCVSCT L

References

[1]

"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL583923 Genomic DNA. Translation: CAC30687.1. Different initiation.
PIR	H87125.
RefSeq	NP_302195.1.
3D structure databases
SMR	Q9CBQ0. Positions 16-706.
ModBase	Search...
Genome annotation databases
GeneID	910759.
KEGG	mle:ML1734.
NMPDR	fig|272631.1.peg.1067.
Organism-specific databases
Leproma	ML1734.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG348953.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1734-MONOMER.
BRENDA	1.17.4.1. 808.
Family and domain databases
InterPro	IPR013346. NrdE_NrdA. IPR013509. Ribncl_Rdtase_lsu_N. IPR000788. Ribncl_red_lg_C. IPR008926. Ribnucl_Rdtase_R1-su_N. 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...

Entry information

Entry name

RIR1_MYCLE

Accession

Primary (citable) accession number: Q9CBQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	August 29, 2001
Last modified:	February 9, 2010
This is version 52 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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