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G4NVG9 (G4NVG9_BACPN) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate By similarity. HAMAP-Rule MF_01683

Catalytic activity

ATP + S-methyl-5-thio-D-ribose = ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01683

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route): step 2/2. HAMAP-Rule MF_01683

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01683

Sequence similarities

Belongs to the methylthioribose kinase family. HAMAP-Rule MF_01683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding115 – 1173ATP By similarity HAMAP-Rule MF_01683
Nucleotide binding250 – 2523ATP By similarity HAMAP-Rule MF_01683

Sites

Binding site441ATP By similarity HAMAP-Rule MF_01683
Binding site611ATP By similarity HAMAP-Rule MF_01683
Binding site2331Substrate By similarity HAMAP-Rule MF_01683
Binding site3401Substrate By similarity HAMAP-Rule MF_01683

Sequences

Sequence LengthMass (Da)Tools
G4NVG9 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: 4D321DB3AF387C54

FASTA39745,133
        10         20         30         40         50         60 
MAVTKTPLYE TLNESSAVAL AVKLGLFPSK STLTCQEIGD GNLNYVFHIY DQEHDRALII 

        70         80         90        100        110        120 
KQAVPYAKVV GESWPLTIDR ARIESSALIR QGEHVPHLVP RVFYSDTEMA VTVMEDLSHL 

       130        140        150        160        170        180 
KIVRKGLIEG EHYPHLSQHI GEFLGKTLFY SSDYALEPKV KKQLVKQFTN PELCDITERL 

       190        200        210        220        230        240 
VFTDPFFDHD TNDFEEELHP FVEKLWNNDN VKIEAAKLKK SFLTSAETLI HGDLHTGSIF 

       250        260        270        280        290        300 
ASEHETKVID PEFAFYGPIG FDVGQFIANL FLNALGRDGG DREPLYHHVK QVWETFQKTF 

       310        320        330        340        350        360 
TEAWEKDSLD VYAKIDGYLT DTLSHIFEEA IGFAGCELIR RAIGLAHVAD LDTIVPFDKR 

       370        380        390 
IGRKRLALET GTAFIEKRSE FKTITDVIEL FQLLVKE 

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References

[1]"Whole-Genome Sequences of Bacillus subtilis and Close Relatives."
Earl A.M., Eppinger M., Fricke W.F., Rosovitz M.J., Rasko D.A., Daugherty S., Losick R., Kolter R., Ravel J.
J. Bacteriol. 194:2378-2379(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: TU-B-10 EMBL AEP86327.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002905 Genomic DNA. Translation: AEP86327.1.
RefSeqYP_004876959.1. NC_016047.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEP86327; AEP86327; GYO_1683.
GeneID11241887.
KEGGbst:GYO_1683.

Phylogenomic databases

KOK00899.

Enzyme and pathway databases

BioCycBSUB1052585:GJWW-1669-MONOMER.
UniPathwayUPA00904; UER00872.

Family and domain databases

HAMAPMF_01683. Salvage_MtnK.
InterProIPR002575. Aminoglycoside_PTrfase.
IPR011009. Kinase-like_dom.
IPR009212. Methylthioribose_kinase.
[Graphical view]
PfamPF01636. APH. 1 hit.
[Graphical view]
PIRSFPIRSF031134. MTRK. 1 hit.
SUPFAMSSF56112. Kinase_like. 1 hit.
TIGRFAMsTIGR01767. MTRK. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG4NVG9_BACPN
AccessionPrimary (citable) accession number: G4NVG9
Entry history
Integrated into UniProtKB/TrEMBL: December 14, 2011
Last sequence update: December 14, 2011
Last modified: April 3, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)