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F0QCU6 (F0QCU6_ACIAP) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 23. Feed History...

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

Sequence length435 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

Region129 – 1324Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site971Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site981Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1691Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1981Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2011Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2231Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2531Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2791Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2241N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
F0QCU6 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: F2F3041F3030DE02

FASTA43546,825
        10         20         30         40         50         60 
MTTLDDCRAL DAHDPLRPLR GHFQLPDGVI YLDGNSLGVL PKAAPARIAE VVAQEWGTDL 

        70         80         90        100        110        120 
IRSWNSASWF DLPQRLGNQL APLIGAGAGE VVCTDSTSIN LYKVLSAALN IAREDAPARR 

       130        140        150        160        170        180 
RIVSERSNFP TDLYIAEGLC RERGLELVLV EPEEIPAALT GDVAVLMLTH VNYRTGAMHD 

       190        200        210        220        230        240 
MAAVTAAAHA QGILCVWDLA HSAGAVPVDL RGAGADFSIG CGYKYLNGGP GAPAFVWVHP 

       250        260        270        280        290        300 
RHADRFWQPL SGWWGHAAPF AFTPDYQPAP GISRYLCGTQ PIISLSALQC GLDVFTAAQP 

       310        320        330        340        350        360 
LGGMQALRAK SLALTDLFIR LVEERCAGHG LGLATPREHA RRGSQVCLTR DEGQGVDGQG 

       370        380        390        400        410        420 
SGAYAIVQAL IARGVIGDFR KGDGGQGPHK DILRFGLTPL YLGFEDVWNA VEHLRAVLDG 

       430 
GEWRRPEFNQ QHAVT 

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References

[1]"Complete sequence of Acidovorax avenae subsp. avenae ATCC 19860."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Gordon S., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19860 / DSM 7227 / JCM 20985 / NCPPB 1011.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002521 Genomic DNA. Translation: ADX45089.1.
RefSeqYP_004233656.1. NC_015138.1.

3D structure databases

ProteinModelPortalF0QCU6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADX45089; ADX45089; Acav_1167.
GeneID10306072.
KEGGaaa:Acav_1167.
PATRIC46836967. VBIAciAve68977_1186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.
OMAVWDLAHS.

Enzyme and pathway databases

BioCycAAVE643561:GHRD-1171-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 nameF0QCU6_ACIAP
AccessionPrimary (citable) accession number: F0QCU6
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: July 9, 2014
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)