nrdB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

NrdB

Synonyms

ribonucleoside diphosphate reductase 1, beta subunit, ferritin-like[1], B2235[2][1], NrdB[2][1] , ECK2227, ftsB, JW2229, b2235

Product description

NrdB[2][3];

Component of B2 protein[2][3]; ribonucleotide reductase I[2]

Ribonucleoside diphosphate reductase, subunit beta; class I, aerobic; ribonucleotide reductase; B2 protein, R2 subunit[4]

EC number (for enzymes)

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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

PMID:13973714[5]

IDA: Inferred from Direct Assay

C

complete

GO:0015949

nucleobase, nucleoside and nucleotide interconversion

PMID:4902211[6]

IDA: Inferred from Direct Assay

P

complete

Contributes to

GO:0004748

ribonucleoside-diphosphate reductase activity

PMID:13973714[5]

IDA: Inferred from Direct Assay

F

complete

Contributes to

GO:0004748

ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor

PMID:13973714[5]

IDA: Inferred from Direct Assay

F

replaces obsoleteGO:0016959

complete

GO:0004748

ribonucleoside-diphosphate reductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000358

F

Seeded from EcoCyc (v14.0)

complete

GO:0004748

ribonucleoside-diphosphate reductase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.17.4.1

F

Seeded from EcoCyc (v14.0)

complete

GO:0005971

ribonucleoside-diphosphate reductase complex

PMID:13973714[5]

IDA: Inferred from Direct Assay

C

complete

GO:0005506

iron ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[7]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0009263

deoxyribonucleotide biosynthetic process

PMID:13973714[5]

IDA: Inferred from Direct Assay

P

complete

GO:0006260

DNA replication

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0235

P

Seeded from EcoCyc (v14.0)

complete

GO:0009186

deoxyribonucleoside diphosphate metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000358

P

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009078

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012348

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000358

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009078

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR012348

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of B2 protein

could be indirect

Protein

dnaN

PMID:15690043[8]

Experiment(s):EBI-881523

Protein

mreB

PMID:15690043[8]

Experiment(s):EBI-881523

Protein

rhsB

PMID:15690043[8]

Experiment(s):EBI-881523

Protein

tufA

PMID:15690043[8]

Experiment(s):EBI-881523

Protein

dnaK

PMID:15690043[8]

Experiment(s):EBI-888955

Protein

tatE

PMID:16606699[9]

Experiment(s):EBI-1142284

Protein

iaaA

PMID:16606699[9]

Experiment(s):EBI-1142284

Protein

nrdA

PMID:16606699[9]

Experiment(s):EBI-1142284

Protein

rhsB

PMID:19402753[10]

MALDI(Z-score):17.053160

Protein

Subunits of ribonucleotide reductase I

could be indirect


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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MAYTTFSQTK NDQLKEPMFF GQPVNVARYD QQKYDIFEKL IEKQLSFFWR PEEVDVSRDR
IDYQALPEHE KHIFISNLKY QTLLDSIQGR SPNVALLPLI SIPELETWVE TWAFSETIHS
RSYTHIIRNI VNDPSVVFDD IVTNEQIQKR AEGISSYYDE LIEMTSYWHL LGEGTHTVNG
KTVTVSLREL KKKLYLCLMS VNALEAIRFY VSFACSFAFA ERELMEGNAK IIRLIARDEA
LHLTGTQHML NLLRSGADDP EMAEIAEECK QECYDLFVQA AQQEKDWADY LFRDGSMIGL
NKDILCQYVE YITNIRMQAV GLDLPFQTRS NPIPWINTWL VSDNVQVAPQ EVEVSSYLVG
QIDSEVDTDD LSNFQL
Length

376

Mol. Wt

43.517 kDa

pI

4.6 (calculated)

Extinction coefficient

62,340 - 62,965 (calc based on 16 Y, 7 W, and 5 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P69924

Domain

22..165

PF00268 Ribonucleotide reductase, small chain

PMID:19920124[11]

Domain

182..336

PF00268 Ribonucleotide reductase, small chain

PMID:19920124[11]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=nrdB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130170

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946732

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0007386

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P69924

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10661

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10661

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946732

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000654

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0655

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 5.2 5.3 5.4 REICHARD, P (1962) Enzymatic synthesis of deoxyribonucleotides. I. Formation of deoxycytidine diphosphate from cytidine diphosphate with enzymes from Escherichia coli. J. Biol. Chem. 237 3513-9 PubMed
  6. Brown, NC & Reichard, P (1969) Ribonucleoside diphosphate reductase. Formation of active and inactive complexes of proteins B1 and B2. J. Mol. Biol. 46 25-38 PubMed
  7. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  8. 8.0 8.1 8.2 8.3 8.4 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  9. 9.0 9.1 9.2 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  10. Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
  11. 11.0 11.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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