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A4J1T0 (A4J1T0_DESRM) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 23. 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 names
EC=4.1.1.19 EMBL ABO49033.1
Gene names
Ordered Locus Names:Dred_0487
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Protein existenceInferred from homology

Ontologies

Keywords
   Molecular functionLyase EMBL ABO49033.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionarginine decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
A4J1T0 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 69D1B9BBBEB92590

FASTA15316,322
        10         20         30         40         50         60 
MLPTPKKYFV TAASSEGKSK LTAFDNALLK ARIGNVNLLR VSSILPPGCQ EDPGMVLPPG 

        70         80         90        100        110        120 
SLVPTAYGYI VSNVPGEIIS ACVGVGINSN DSFGVIMEFS GKCSKEEAEQ NITNMVKEAF 

       130        140        150 
ETRGMELKDI KIASAEHKVE KIGCALAAVP LWY 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO49033.1.
RefSeqYP_001111858.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J1T0.
SMRA4J1T0. Positions 3-42.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4J1T0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4956912.
GenomeReviewsGene locus Dred_0487 in contig CP000612_GR.
KEGGdrm:Dred_0487.
PATRIC21726839. VBIDesRed82656_0517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1945.
HOGENOMHBG539680.
OMALVPTAYG.
ProtClustDBPRK01285.

Family and domain databases

HAMAPMF_01404. PvlArgDC.
[Tree]
InterProIPR016104. Pyr-dep_his/arg-deCO2ase.
IPR016105. Pyr-dep_his/arg-deCO2ase_sand.
IPR002724. Pyruvoyl-dep_arg_deCO2ase.
[Graphical view]
Gene3DG3DSA:3.50.20.10. Pyr-dep_his/arg-deCO2ase_sand. 1 hit.
KOK02626.
PfamPF01862. PvlArgDC. 1 hit.
[Graphical view]
PIRSFPIRSF005216. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
ProDomPD010449. Pyruvoyl-dep_arg_deCO2ase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56271. His_carbxylase. 1 hit.
TIGRFAMsTIGR00286. TIGR00286. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA4J1T0_DESRM
AccessionPrimary (citable) accession number: A4J1T0
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: December 14, 2011
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)