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Q254T2 (Q254T2_CHLFF) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 51. Feed History...

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

Sequence length425 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

Region134 – 1374Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1061Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1071Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2191Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2221Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2441Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2741Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site3041Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2451N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
Q254T2 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: B7A83B4A7BE08193

FASTA42548,438
        10         20         30         40         50         60 
MNEILKNYQK KATQLDEQDC LKHLRARFSL PKDPNAIYFC NNSLGLPAVS AFTKIEELLQ 

        70         80         90        100        110        120 
CWSDVGVNGW FEGTGNWYRS FDRPLRQPLS KILGAEYEEV IVMNSLTMNL HLLLVSFYRP 

       130        140        150        160        170        180 
TDTRYKILIE GPTFPSDLYA IKSHLSFHGR NPDEALIILK PRADEDLLRY EDFQQILKEQ 

       190        200        210        220        230        240 
GESIALVFMN CVNFLTGQVL EVEAITHLAK EKGCIVGCDL AHAAGNIPLK LHEWGVDFAL 

       250        260        270        280        290        300 
GCSYKYLCGG PGGPGIAYVH KSHHDEQLPR FSGWWGNDPE TRFQMQLQPE FVPYGGAYSW 

       310        320        330        340        350        360 
QVSTPSILSL MPLLATLEVF EEAGMERVRN KSKQMTAFLL ELLELAPSSY FEIITPRDPE 

       370        380        390        400        410        420 
LRGSQLSVRI QQHSEEVLQK LEAQRITCDS RPPDIIRVTP TPLYNTFSEI YQFTCKLLEV 


LEIKL 

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References

[1]"Genome sequence of the cat pathogen, Chlamydophila felis."
Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H., Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H., Hattori M., Kuhara S., Shirai M.
DNA Res. 13:15-23(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fe/C-56 EMBL BAE81206.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006861 Genomic DNA. Translation: BAE81206.1.
RefSeqYP_515351.1. NC_007899.1.

3D structure databases

ProteinModelPortalQ254T2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264202.CF0434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3958709.
KEGGcfe:CF0434.
PATRIC20204482. VBIChlFel51660_0452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.
ProtClustDBCLSK2485142.

Enzyme and pathway databases

BioCycCFEL264202:GJCG-454-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 nameQ254T2_CHLFF
AccessionPrimary (citable) accession number: Q254T2
Entry history
Integrated into UniProtKB/TrEMBL: April 18, 2006
Last sequence update: April 18, 2006
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)