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C3H1U6 (C3H1U6_BACTU) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 12. 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
Gene names
ORF Names:bthur0011_24310 EMBL EEM83519.1
OrganismBacillus thuringiensis serovar huazhongensis BGSC 4BD1 EMBL EEM83519.1
Taxonomic identifier527030 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine By similarity. SAAS SAAS017484

Catalytic activity

N-formyl-L-kynurenine + H2O = formate + L-kynurenine. SAAS SAAS017484

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2. SAAS SAAS017484

Ontologies

Keywords
   Biological processTryptophan catabolism SAAS SAAS017484
   Molecular functionHydrolase SAAS SAAS017484 EMBL EEM83519.1
Gene Ontology (GO)
   Biological processtryptophan catabolic process to kynurenine

Inferred from electronic annotation. Source: InterPro

   Molecular functionformamidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
C3H1U6 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 54270A35415116A0

FASTA20923,066
        10         20         30         40         50         60 
MKTSEWIDIS QPLNNNIATW PGDTPFSYEV SWSKEESGSV NVGKLTMSIH TGTHIDAPFH 

        70         80         90        100        110        120 
FDNDGKKVLD LDVQVYVGPA RIIDVSNLES IGKKELESFH LEGVERLLLR TSSHGKAEEF 

       130        140        150        160        170        180 
PEVIPHLRAD IASFLSEKGI RLIGVDVPSV DPLDDKELAA HHQLFKHGIH ILENVVLDHV 

       190        200 
ADGDYELIAL PLALTDADGS PVRAVIRPI 

« Hide

References

[1]"Annotation of the Bacillus thuringiensis BGSC 4BD1 genome."
Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BGSC 4BD1 EMBL EEM83519.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACNI01000059 Genomic DNA. Translation: EEM83519.1.

3D structure databases

ProteinModelPortalC3H1U6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000163286; EBBACP00000158742; EBBACG00000167150.
PATRIC26159934. VBIBacThu93808_4081.

Family and domain databases

InterProIPR017484. Arylformamidase.
IPR007325. Cyclase.
[Graphical view]
PfamPF04199. Cyclase. 1 hit.
[Graphical view]
TIGRFAMsTIGR03035. Trp_arylform. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC3H1U6_BACTU
AccessionPrimary (citable) accession number: C3H1U6
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)