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B2SY85 (B2SY85_BURPP) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 41. 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 length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_01970

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800 HAMAP-Rule MF_01970

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region129 – 1324Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site971Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site981Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1721Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2011Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2041Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2261Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2561Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2821Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2271N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
B2SY85 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: E6B02CF0CDA4D46C

FASTA41645,893
        10         20         30         40         50         60 
MNHRDEALAL DSADPLATLR DQFALSSTTI YLDGNSLGVP PAAAAQRAQT VIGAEWGEGL 

        70         80         90        100        110        120 
IRSWNTAGWF ELPRRLGNKL APLIGAAENE VVVTDTISIN LFKLLSAAVR VANERDPKRR 

       130        140        150        160        170        180 
VIVSERSNFP TDLYIAQGLI EQLDRGYELR LVDDPSELPA AIGDDTAIAM ITHVNYRTGY 

       190        200        210        220        230        240 
MHDMAALTKL IHDKGALALW DLAHSAGAVP VDLNGVGADY AVGCTYKYLN GGPGSPAFVW 

       250        260        270        280        290        300 
VPKRHQNEFA QPLSGWWGHR APFKMDPAYQ PDDGIGRFLC GTQPMVSMSL VECGLDVFLQ 

       310        320        330        340        350        360 
TDMQAVRKKS LALTDLFIEL VEARCSEFPL TLVTPREHAQ RGSHASFEHP HGYEVMQALI 

       370        380        390        400        410 
ARGVIGDYRE PHVLRFGFTP LYTRFVDVWD AVETLREVLV KETWRAPEFA ARGAVT 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001052 Genomic DNA. Translation: ACD17620.1.
RefSeqYP_001896844.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2SY85.
SMRB2SY85. Positions 4-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398527.Bphyt_3228.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD17620; ACD17620; Bphyt_3228.
GeneID6280896.
KEGGbpy:Bphyt_3228.
PATRIC19216958. VBIBurPhy117947_7227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycBPHY398527:GJEX-3273-MONOMER.
UniPathwayUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_01970. Kynureninase.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR14084. PTHR14084. 1 hit.
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF038800. KYNU. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB2SY85_BURPP
AccessionPrimary (citable) accession number: B2SY85
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: July 9, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)