Q9PL92 (RIR2_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleoside-diphosphate reductase subunit beta
EC=1.17.4.1

Alternative name(s):
Ribonucleotide reductase small subunit

Gene names

Name:	nrdB
Ordered Locus Names:	TC_0215

Organism

Chlamydia muridarum (strain MoPn / Nigg) [Complete proteome] [HAMAP]

Taxonomic identifier

243161 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Chlamydiae/Verrucomicrobia group › Chlamydiae › Chlamydiia › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia › Chlamydia muridarum

Protein attributes

Sequence length	346 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.
Cofactor	Binds 2 iron ions per subunit 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 small chain family.

Ontologies

Keywords
Biological process	DNA replication
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-UniPathway deoxyribonucleoside diphosphate metabolic process Inferred from electronic annotation. Source: InterPro deoxyribonucleotide biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	ribonucleoside-diphosphate reductase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Inferred from electronic annotation. Source: EC transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Ribonucleoside-diphosphate reductase subunit beta		PRO_0000190473
Sites
	Active site	129	1	By similarity
	Metal binding	89	1	Iron 1 By similarity
	Metal binding	120	1	Iron 1 By similarity
	Metal binding	120	1	Iron 2 By similarity
	Metal binding	123	1	Iron 1 By similarity
	Metal binding	193	1	Iron 2 By similarity
	Metal binding	227	1	Iron 2 By similarity
	Metal binding	230	1	Iron 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9PL92 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C5AF2C3372FBDA57	FASTA	346	40,488
	10 20 30 40 50 60 MQADILDGKQ KRVNLNSKRL VNCNQVDVNQ LVPIKYKWAW EHYLNGCANN WLPTEISMGK 70 80 90 100 110 120 DIELWKSNVL SEDERRVILL NLGFFSTAES LVGNNIVLAI FKHVTNPEAR QYLLRQAFEE 130 140 150 160 170 180 AVHTHTFLYI CESLGLDEKE IFNAYNERAS IKAKDDFQME ITGKVLDPNF RTDSVEGLQE 190 200 210 220 230 240 FIKNLVGYYI IMEGIFFYSG FVMILSFHRQ NKMVGIGEQY QYILRDETIH LNFGVDLING 250 260 270 280 290 300 IKEENPEIWT TELQQEIIEM IQRAVDLEID YARDCLPRGI LGLRASMFID YVQHIADRRL 310 320 330 340 ERIGLKPIYH TKNPFPWMSE TIDLNKEKNF FETRVTEYQH AASLTW

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39087.1.
PIR	G81728.
RefSeq	NP_296594.1. NC_002620.2.
3D structure databases
ProteinModelPortal	Q9PL92.
SMR	Q9PL92. Positions 2-318.
ModBase	Search...
Protein-protein interaction databases
STRING	243161.TC0215.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF39087; AAF39087; TC_0215.
GeneID	1246341.
KEGG	cmu:TC0215.
PATRIC	20371812. VBIChlMur19118_0235.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0208.
KO	K00526.
OMA	ICNRRCQ.
ProtClustDB	PRK07209.
Enzyme and pathway databases
BioCyc	CMUR243161:GHYU-226-MONOMER.
UniPathway	UPA00326.
Family and domain databases
Gene3D	1.10.620.20. 1 hit.
InterPro	IPR009078. Ferritin-like_SF. IPR012348. RNR-rel. IPR026023. RNR_bsu_prok. IPR000358. RNR_small. [Graphical view]
PANTHER	PTHR23409. PTHR23409. 1 hit.
Pfam	PF00268. Ribonuc_red_sm. 1 hit. [Graphical view]
PIRSF	PIRSF000355. NrdB. 1 hit.
SUPFAM	SSF47240. Ferritin/RR_like. 1 hit.
PROSITE	PS00368. RIBORED_SMALL. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIR2_CHLMU

Accession

Primary (citable) accession number: Q9PL92

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program