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Q2S2F5 (KYNB_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kynurenine formamidase

Short name=KFA
EC=3.5.1.9
Alternative name(s):
N-formylkynurenine formamidase
Gene names
Name:kynB
Ordered Locus Names:SRU_1503
OrganismSalinibacter ruber (strain DSM 13855 / M31)
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

Sequence similarities

Belongs to the kynB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Kynurenine formamidase
PRO_0000362138

Sequences

Sequence LengthMass (Da)Tools
Q2S2F5 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 8882F8F51EB21EF5

FASTA21222,347
        10         20         30         40         50         60 
MALIDISRSV SPATAVWPGD QEVQWTWTAR RNEDESSVNL GSLRLSTHTG THVDAPLHVK 

        70         80         90        100        110        120 
RQGQATDDLP LDSFVGPARV VDVNANAPSV RPEHIGQLDG ASAERVLFKT SSGVSPDDEW 

       130        140        150        160        170        180 
PDAVVPIQPD TIHALADAGV SLVGTDAPSV DPLDSTDLPA HHALLDTGIV NLEGLVLTNV 

       190        200        210 
PPGRYELIAL PLKIVGGDAA PVRAVLRDAP DP 

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000159 Genomic DNA. Translation: ABC46272.1.
RefSeqYP_445626.1. NC_007677.1.

3D structure databases

ProteinModelPortalQ2S2F5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2S2F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3852572.
GenomeReviewsGene locus SRU_1503 in contig CP000159_GR.
KEGGsru:SRU_1503.
NMPDRfig|309807.5.peg.1419.
PATRIC23425441. VBISalRub86502_1559.
TIGRSRU_1503.

Phylogenomic databases

eggNOGCOG1878.
HOGENOMHBG686791.
OMAHTSKWPL.
PhylomeDBQ2S2F5.
ProtClustDBCLSK2775289.

Enzyme and pathway databases

BioCycSRUB309807:SRU_1503-MONOMER.

Family and domain databases

InterProIPR007325. Cyclase.
[Graphical view]
KOK07130.
PfamPF04199. Cyclase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKYNB_SALRD
AccessionPrimary (citable) accession number: Q2S2F5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families