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G0K5W2 (G0K5W2_STEMA) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length424 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

Region133 – 1364Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1051Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1061Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2181Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2211Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2431Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2741Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site3021Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2441N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
G0K5W2 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: A9DED9F234B82790

FASTA42446,900
        10         20         30         40         50         60 
MSDLLSRTHA IALDAADPLR SLRNEFLIPR HGGGEQTYFV GNSLGLQPRG AQAAVQEVMK 

        70         80         90        100        110        120 
QWGELAVEGH FTGPTQWLSY HRLVSAQLAR VVGALPSEVV AMNTLSVNLH LMMVSFYRPT 

       130        140        150        160        170        180 
AQRPVILMEA GAFPTDRHAV EAQIRFHGFD PAECLVEVQP DEANGTISLN AIERAITEHG 

       190        200        210        220        230        240 
PRLALVLWPG VQYRTGQAFD LDAITRAARL QGARIGFDLA HSVGNLPLRL HDVAPDFAVW 

       250        260        270        280        290        300 
CHYKYLNSGP GAVAGAFVHE RHHRDTTLPR FAGWWGHEEA TRFQMAPQFT PAIGAEGWQL 

       310        320        330        340        350        360 
SNPPILGLAP LRASLDLFER AGMEALRSKS LALTGMLEAL VRARLPQVLD IITPADPQRR 

       370        380        390        400        410        420 
GCQLSLRVIG GRERGRALFE HLRGIGVLGD WREPDVIRIS PTPLYNRYLD VHHFVEEVEA 


WAGL 

« Hide

References

[1]"Complete sequence of Stenotrophomonas maltophilia JV3."
US DOE Joint Genome Institute
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Medau R. expand/collapse author list , Furlan B., Mui Tsai S., Rodriques J., Tiedje J., Woyke T.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: JV3 EMBL AEM51931.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002986 Genomic DNA. Translation: AEM51931.1.
RefSeqYP_004793157.1. NC_015947.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEM51931; AEM51931; BurJV3_2611.
GeneID11047375.
KEGGbuj:BurJV3_2611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

BioCycSMAL868597:GHCG-2673-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 nameG0K5W2_STEMA
AccessionPrimary (citable) accession number: G0K5W2
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: February 19, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)