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G2M026 (G2M026_9XANT) Unreviewed, UniProtKB/TrEMBL

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

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

Sequence length423 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 site2731Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site3011Pyridoxal 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
G2M026 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 947C6288ED667A63

FASTA42345,909
        10         20         30         40         50         60 
MTDLLSRAHA AALDAADPLR GLRDAFVFPQ HGDDDQTYFV GNSLGLQPRA ARAMVDEVLD 

        70         80         90        100        110        120 
RWGALAVEGH FTGPTQWLTY HQLVRDGLAR VVGAQPGEVV AMNTLSVNLH LMMASFYRPT 

       130        140        150        160        170        180 
AERGAILIEA GAFPSDRHAV ESQLRLHGLD PATHLIEVDA DEPNGTVSMT AIAEAIAQHG 

       190        200        210        220        230        240 
PRLALVLWPG IQYRTGQAFD LAEIVRLARA QGAAVGFDLA HAVGNLPLTL HDDGVDFAVW 

       250        260        270        280        290        300 
CHYKYLNAGP GAVGGCFVHA RHANSDLPRM AGWWGHEQQT RFRMDPQFVP SPGAEGWQLS 

       310        320        330        340        350        360 
NPPVLALAPL RASLALFDQA GMAALRAKSE QLTGHLEQLI HARVPQVLQI VTPAEPARRG 

       370        380        390        400        410        420 
CQLSLRVAGG RAKGRALFEH LHAAGVLGDW REPDVIRIAP VPLYNRFSDL HTFVEQVEAW 


AAA 

« Hide

References

[1]"Comparative Genomic Analysis of Xanthomonas axonopodis pv. citrumelo F1, Which Causes Citrus Bacterial Spot Disease, and Related Strains Provides Insights into Virulence and Host Specificity."
Jalan N., Aritua V., Kumar D., Yu F., Jones J.B., Graham J.H., Setubal J.C., Wang N.
J. Bacteriol. 193:6342-6357(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: F1 EMBL AEO41854.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002914 Genomic DNA. Translation: AEO41854.1.
RefSeqYP_004851152.1. NC_016010.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEO41854; AEO41854; XACM_1573.
GeneID11132486.
KEGGxax:XACM_1573.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

BioCycXALF981368:GH9H-1573-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 nameG2M026_9XANT
AccessionPrimary (citable) accession number: G2M026
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: February 19, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)