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J7QH41 (J7QH41_BORP1) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 11. 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 existenceInferred from homology

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 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
J7QH41 [UniParc].

Last modified October 31, 2012. Version 1.
Checksum: 7DCA08DCDD5AA37B

FASTA41645,694
        10         20         30         40         50         60 
MTTRQACLEA DRRDPLAAFK DEFELPAGLI YLDGNSLGAL PRGAAARAAQ VIGQEWGQGL 

        70         80         90        100        110        120 
IRSWNTAGWF ELPARLGNKL AGLIGAGQDE VVMTDSTSLN IFKALAAALR LAQRAAPQRK 

       130        140        150        160        170        180 
VIVSERDNFP TDLYMIQGMI DLLRQGYELR LVDAGLSLEQ ALDDDVAVVL LSHVNYRTGA 

       190        200        210        220        230        240 
MHDMAAVSRR AHARGALIIW DLAHAAGAVP VALDADGADF AVGCTYKYLN GGPGSPAFIW 

       250        260        270        280        290        300 
VAPRHRDDFW QPLSGWWGHR QPFEMADTYV PAQGIRRYLC GTQPIVSLAT AECGLDIALR 

       310        320        330        340        350        360 
ADIAQVRAKS LALGDRFIAL VESRCADHPL TLATPREHAR RGSHVSFLHP QGYAVMQALI 

       370        380        390        400        410 
ARGVIGDYRE PELLRFGLTP LYLSHADIWD AVEILREVLD TRAWDRPQYR ERAAVT 

« Hide

References

[1]"Comparative genomics of the classical Bordetella subspecies: the evolution and exchange of virulence-associated diversity amongst closely related pathogens."
Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M., Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.
BMC Genomics 13:545-545(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9797 / DSM 5571 / NCTC 10739 / 18323.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE965805 Genomic DNA. Translation: CCJ64940.1.
RefSeqYP_006627955.1. NC_018518.1.

3D structure databases

ProteinModelPortalJ7QH41.
SMRJ7QH41. Positions 2-404.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCJ64940; CCJ64940; BN118_3515.
GeneID13803207.
KEGGbper:BN118_3515.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

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 nameJ7QH41_BORP1
AccessionPrimary (citable) accession number: J7QH41
Entry history
Integrated into UniProtKB/TrEMBL: October 31, 2012
Last sequence update: October 31, 2012
Last modified: February 19, 2014
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)