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D3P4C7 (D3P4C7_AZOS1) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Kynureninase PIRNR PIRNR038800 HAMAP-Rule MF_01970

EC=3.7.1.3 PIRNR PIRNR038800 HAMAP-Rule MF_01970
Alternative name(s):
L-kynurenine hydrolase HAMAP-Rule MF_01970
Gene names
Name:kynU HAMAP-Rule MF_01970
Ordered Locus Names:AZL_c02130 EMBL BAI75506.1
Encoded onPlasmid pAB510c Ref.1 EMBL BAI75506.1
OrganismAzospirillum sp. (strain B510) [Complete proteome] [HAMAP] EMBL BAI75506.1
Taxonomic identifier137722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length397 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

Region113 – 1164Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site851Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site861Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1551Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1841Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1871Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2091Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2391Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2651Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2101N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
D3P4C7 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: 7B9F4C078D5B12DF

FASTA39742,670
        10         20         30         40         50         60 
MTDFAKTRAR FDIPDGVIYL DGNSLGPLPI AAKERVARTL AEEWGGQLIR GWNSAGWMVQ 

        70         80         90        100        110        120 
PRKVGDRIAR LIGAPAGSVV VGDTLSIKVY QALAAALAMR PERRVILSDS GNFPTDLYMA 

       130        140        150        160        170        180 
EGLIETLGQG HILKVVAPEE VEGTIGEDVA VLMLTEVDYR TGRLHDMAAL TAKAHAAGVV 

       190        200        210        220        230        240 
TVWDLAHSAG ALPVDLAGAG TDFAVGCTYK YLNGGPGAPA FIYVAPQHAE RARPALSGWM 

       250        260        270        280        290        300 
GHEAPFAFDP SYRPGAGVER MRVGTPPVIA LAALDAALDV WDDVDMADIR RTSMTLCDLF 

       310        320        330        340        350        360 
IELVEAQCPT LELASPRDGS RRGSQVSFRH PQGYAIMQAL IDRGVIGDFR APDVLRFGFT 

       370        380        390 
PLYIGEAEVR GAVAVLKQVT DGGLWDRPEY HRKAIVT 

« Hide

References

[1]"Complete genomic structure of the cultivated rice endophyte Azospirillum sp. B510."
Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H., Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N., Nakayama S. expand/collapse author list , Yamada M., Tabata S., Sato S.
DNA Res. 17:37-50(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B510 EMBL BAI75506.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010949 Genomic DNA. Translation: BAI75506.1.
RefSeqYP_003452050.1. NC_013857.1.

3D structure databases

ProteinModelPortalD3P4C7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI75506; BAI75506; AZL_c02130.
GeneID8795090.
KEGGazl:AZL_c02130.
PATRIC31939342. VBIAzoSp82869_5243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000242437.
KOK01556.

Enzyme and pathway databases

BioCycASP137722:GBYD-4956-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 nameD3P4C7_AZOS1
AccessionPrimary (citable) accession number: D3P4C7
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: July 9, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)