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E3HSW2 (E3HSW2_ACHXA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 24. 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
E3HSW2 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: AE2B2EED914FF224

FASTA41645,951
        10         20         30         40         50         60 
MNTRDACVNA DRQDPLAPLK DRFDLPPGVL YMDGNSLGVL PKDAAARAAA VIGQEWGTGL 

        70         80         90        100        110        120 
IRSWNTAGWF ELPARLGDKL GRLLGAREGE LVVTDTTSLN IFKALAAALR IQQHQHPQRR 

       130        140        150        160        170        180 
VILSERDNFP TDLYMIQGMI DLLQQGYEMR LIDDELPLEK ALDESVAVML LSHVNYRSGQ 

       190        200        210        220        230        240 
MHDMAAVTAL AHERGALAIW DLAHAAGAVP VDLNGANADF AVGCTYKYLN GGPGSPAFIW 

       250        260        270        280        290        300 
VAPRHTKDFW QPLSGWWGHT RPFDMAVAYE PAGGVRRYLC GTQPIVSLSL VECGLDVAHA 

       310        320        330        340        350        360 
ADMAEVRKKS LALGDLFIAL VEERCAEHPL TLVTPRKHAD RGSHVSFRHP NGFEVMQALI 

       370        380        390        400        410 
ARGVIGDYRE PEVLRFGLTP LYFGYADVWD AVDILKDVLD TRSWDKPEFK HRAAVT 

« Hide

References

[1]"Complete genome sequence of the haloaromatic acids-degrading bacterium Achromobacter xylosoxidans A8."
Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.
J. Bacteriol. 193:791-792(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A8 EMBL ADP18563.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002287 Genomic DNA. Translation: ADP18563.1.
RefSeqYP_003981278.1. NC_014640.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADP18563; ADP18563; AXYL_05263.
GeneID9899595.
KEGGaxy:AXYL_05263.
PATRIC42563608. VBIAchXyl160325_5263.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.

Enzyme and pathway databases

BioCycAXYL762376:GJUB-5263-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 nameE3HSW2_ACHXA
AccessionPrimary (citable) accession number: E3HSW2
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: February 19, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)