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Protein
Submitted name:

NimA-related protein

Gene

DR_0842

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711PyruvateCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

PyruvateCombined sources

Enzyme and pathway databases

BioCyciDRAD243230:GH46-864-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
NimA-related proteinImported
Gene namesi
Ordered Locus Names:DR_0842Imported
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)Imported
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Pathology & Biotechi

Chemistry

DrugBankiDB04398. Lactic Acid.

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_0842.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W3OX-ray1.60A1-195[»]
1W3PX-ray1.80A1-195[»]
1W3QX-ray1.88A1-195[»]
1W3RX-ray1.90A1-195[»]
2VPAX-ray1.20A1-195[»]
2X1JX-ray1.90A2-195[»]
2X1KX-ray1.55A2-195[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RW27.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1082Pyruvate bindingCombined sources

Phylogenomic databases

eggNOGiCOG3467. LUCA.
HOGENOMiHOG000153413.
InParanoidiQ9RW27.
KOiK07005.
OMAiWSGKENW.
OrthoDBiEOG65XN12.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR024747. Pyridox_Oxase-rel.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF12900. Pyridox_ox_2. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9RW27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDFYDPRER DPSVSRRPQN RQSDEWIREL LLRGTIARVA TLWQGEDGAA
60 70 80 90 100
FPFITPLAYA YRPEQGDLVY HTNVVGRLRA NAGQGHPATL EVSEIGQFLP
110 120 130 140 150
SNSPLELSVQ YRSVMVFGTA RVLAGEDARA ALTTLSERVF PGLKVGETTR
160 170 180 190
PISEDDLKRT SVYSLSIDRW SGKENWAEQA IQEEDWPALG PEWLG
Length:195
Mass (Da):21,890
Last modified:May 1, 2000 - v1
Checksum:i87E12269320F961C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10419.1.
PIRiF75469.
RefSeqiNP_294566.1. NC_001263.1.
WP_010887488.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF10419; AAF10419; DR_0842.
GeneIDi1799981.
KEGGidra:DR_0842.
PATRICi21629238. VBIDeiRad64572_1025.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10419.1.
PIRiF75469.
RefSeqiNP_294566.1. NC_001263.1.
WP_010887488.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W3OX-ray1.60A1-195[»]
1W3PX-ray1.80A1-195[»]
1W3QX-ray1.88A1-195[»]
1W3RX-ray1.90A1-195[»]
2VPAX-ray1.20A1-195[»]
2X1JX-ray1.90A2-195[»]
2X1KX-ray1.55A2-195[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0842.

Chemistry

DrugBankiDB04398. Lactic Acid.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF10419; AAF10419; DR_0842.
GeneIDi1799981.
KEGGidra:DR_0842.
PATRICi21629238. VBIDeiRad64572_1025.

Phylogenomic databases

eggNOGiCOG3467. LUCA.
HOGENOMiHOG000153413.
InParanoidiQ9RW27.
KOiK07005.
OMAiWSGKENW.
OrthoDBiEOG65XN12.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-864-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RW27.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR024747. Pyridox_Oxase-rel.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF12900. Pyridox_ox_2. 1 hit.
[Graphical view]
SUPFAMiSSF50475. SSF50475. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422Imported.
  2. "Structural basis of 5-nitroimidazole antibiotic resistance: the crystal structure of NimA from Deinococcus radiodurans."
    Leiros H.K., Kozielski-Stuhrmann S., Kapp U., Terradot L., Leonard G.A., McSweeney S.M.
    J. Biol. Chem. 279:55840-55849(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
  3. "High-resolution structure of the antibiotic resistance protein NimA from Deinococcus radiodurans."
    Leiros H.K., Tedesco C., McSweeney S.M.
    Acta Crystallogr. F 64:442-447(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH PYRUVATE.
  4. "Biophysical characterization and mutational analysis of the antibiotic resistance protein NimA from Deinococcus radiodurans."
    Leiros H.K., Brandsdal B.O., McSweeney S.M.
    Biochim. Biophys. Acta 1804:967-976(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-195.

Entry informationi

Entry nameiQ9RW27_DEIRA
AccessioniPrimary (citable) accession number: Q9RW27
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.