Reviewed, UniProtKB/Swiss-Prot P0A5W8 (RIR1_MYCTU)

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:	Rv3051c, MT3137
ORF Names:	MTV012.66c

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	725 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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 – 725	725	Ribonucleoside-diphosphate reductase subunit alpha		PRO_0000187221
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
Experimental info
	Sequence conflict	230 – 231	2	AP → GA in AAA64444. Ref.3
	Sequence conflict	457 – 458	2	SD → RH in AAA64444. Ref.3
	Sequence conflict	622	1	I → V in AAA64444. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P0A5W8-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 38C315D149331D55	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Isolation of ribonucleotide reductase from Mycobacterium tuberculosis and cloning, expression, and purification of the large subunit." Yang F., Lu G., Rubin H. J. Bacteriol. 176:6738-6743(1994) [PubMed: 7961427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-725. Strain: ATCC 35801 / TMC 107 / Erdman.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842581 Genomic DNA. Translation: CAA16136.1. Different initiation. AE000516 Genomic DNA. Translation: AAK47468.1. L34407 Genomic DNA. Translation: AAA64444.1.
PIR	F70861.
RefSeq	NP_217567.1. NP_337654.1.
3D structure databases
SMR	P0A5W8. Positions 26-710.
ModBase	Search...
Genome annotation databases
GeneID	888869. 923996.
GenomeReviews	Gene locus MT3137 in contig AE000516_GR. Gene locus Rv3051c in contig AL123456_GR.
KEGG	mtc:MT3137. mtu:Rv3051c.
TIGR	MT3137.
Organism-specific databases
TubercuList	Rv3051c.
Phylogenomic databases
HOGENOM	P0A5W8.
OMA	HIPTQDD.
Enzyme and pathway databases
BRENDA	1.17.4.1. 809.
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...

Entry information

Entry name

RIR1_MYCTU

Accession

Primary (citable) accession number: P0A5W8
Secondary accession number(s): O53296, P50640

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	November 3, 2009
This is version 32 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)