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A4WSW3 (A4WSW3_RHOS5) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 47. 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 length400 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

Region117 – 1204Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site891Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site901Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1581Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1871Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1901Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2121Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2421Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2681Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2131N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
A4WSW3 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: B76C43921F6DC989

FASTA40043,329
        10         20         30         40         50         60 
MEGAMTDFEA TRAMFDLPEG VIYLDGNSLG PLPRAAAARV AACVTEEWGG MLVTGWNRAG 

        70         80         90        100        110        120 
WMEMPRRLGD RIGRLVGAEP GTVVLGDTLS IKVFQALAAA CEMRPGRRVI LSDSGNFPSD 

       130        140        150        160        170        180 
LYMAEGLCRM LGDRELRLVA PEEVEGAITD ELAAVMVTEV DYRTGRRHDM AAITAKAHAA 

       190        200        210        220        230        240 
GALAIWDLAH SAGALPVRVA EDGADFAVGC TYKYLNSGPG GPAFIYVAPR HGERAVPALS 

       250        260        270        280        290        300 
GWLGHAAPFA FDLAYRPGRG VERMRVGTPP VIQMAALDAA LDVWDGVDLA RLRTRSLELT 

       310        320        330        340        350        360 
DLFIAEVETR CPELALATPR DHARRGSQVS FRHPEGYPIM QALIARGVIG DFRAPDILRF 

       370        380        390        400 
GFTPLYIGPA EVVRAAAILS EVMEGRLWDR EDYRQRAAVT 

« Hide

References

[1]"Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17025 / ATH 2.4.3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000661 Genomic DNA. Translation: ABP70477.1.
RefSeqYP_001167782.1. NC_009428.1.

3D structure databases

ProteinModelPortalA4WSW3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349102.Rsph17025_1584.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP70477; ABP70477; Rsph17025_1584.
GeneID5082395.
KEGGrsq:Rsph17025_1584.
PATRIC23161418. VBIRhoSph94549_1633.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycRSPH349102:GHE1-2911-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 nameA4WSW3_RHOS5
AccessionPrimary (citable) accession number: A4WSW3
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)