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C7PNU8 (C7PNU8_CHIPD) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 27. Feed History...

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

Sequence length421 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

Region132 – 1354Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1041Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1051Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2171Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2201Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2421Pyridoxal 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 residue2431N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
C7PNU8 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: 7D769B2A1FAF59E2

FASTA42148,196
        10         20         30         40         50         60 
MFELSRRFAE EQDQSDPLKT YREQFYFPQR NGKDAIYFCG NSLGLQPKNV KPAIEQELND 

        70         80         90        100        110        120 
WKHHAVEGYW NAENPWLYYQ QYCSKPLTKI VGASQEELTV MNTLTVNLHL LLMSFYQPTK 

       130        140        150        160        170        180 
QRFKVLMEAG AFPSDQYALE TQVRLHGYNP AEAIIEVAPR PGERLIREED IFEIIERESS 

       190        200        210        220        230        240 
SLAIILLGGI NYYTGQLFNM QSITEVAHRV GAIVGFDLAH VVGNVPLNLH DWEVDFAVWC 

       250        260        270        280        290        300 
SYKYLNGGPG AVGGAFIHEK HALDTNRQRL GGWWGNEEST RFKMEKGFKP KNRAEGWQIS 

       310        320        330        340        350        360 
TAQVFNMVAL KASLELFESA GMAALRDKSI KLTNYLEFLL KHIENIKFEI ITPKNCKERG 

       370        380        390        400        410        420 
AQLSLLFHEK GREIQQKMTD AGIIVDWREP GVIRISPAPL YNSYGDVFHF YEIIANIDSN 


A

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References

[1]"The complete genome of Chitinophaga pinensis DSM 2588."
US DOE Joint Genome Institute (JGI-PGF)
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Sims D., Meinche L., Brettin T., Detter J.C., Han C. expand/collapse author list , Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A.
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43595 / DSM 2588 / NCIB 11800 / UQM 2034.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001699 Genomic DNA. Translation: ACU58645.1.
RefSeqYP_003120846.1. NC_013132.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING485918.Cpin_1147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU58645; ACU58645; Cpin_1147.
GeneID8357263.
KEGGcpi:Cpin_1147.
PATRIC21350917. VBIChiPin99107_1135.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAMVSFYRP.

Enzyme and pathway databases

BioCycCPIN485918:GHYR-1166-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. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01814. kynureninase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC7PNU8_CHIPD
AccessionPrimary (citable) accession number: C7PNU8
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: May 29, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info