Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

D3Q6N0 (D3Q6N0_STANL) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 30. 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

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

Region130 – 1334Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1011Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1021Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2071Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2101Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2321Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2621Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2881Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2331N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
D3Q6N0 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: 7BC55DD854AE93A8

FASTA42145,824
        10         20         30         40         50         60 
MFSELHPEAD PATLDAADPL ASFRSEFAHD TEDLIYLDGN SLGRPPRAVL DAVRRVTDEE 

        70         80         90        100        110        120 
WTNRLIRGWD EWIELPSRAG DALAADVVGA RPGEVLVCDS TSVNLYKLAA AALDAAPKGR 

       130        140        150        160        170        180 
RVIVTDDDNF PTDRYILAGI AERHGGELRV IHTDIDEGVD PKTVAKAVKK DTALLCLSHV 

       190        200        210        220        230        240 
SYRSGAIADM AAITERAHKS GAKVLWDLCH SAGAVPVELD ACGVDLAVGC TYKYLNAGPG 

       250        260        270        280        290        300 
APAFLYVREE LQTRLRQPMW GWFSQTDQFA MGPEYLPRED IGRFAVGTPT VVGVAAVEAA 

       310        320        330        340        350        360 
VAVTARAGVA ALREKSVRLG AYAQALFAEW LAPLGFELAS PDDPLRRGGH LTLAHKEAWR 

       370        380        390        400        410        420 
IGQAMRARGV IPDYREPDRL RLGFAPLYNG YRDVHEGLSR VADIVRSGEY EKFPAEKGQV 


T 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001778 Genomic DNA. Translation: ADD44273.1.
RefSeqYP_003513366.1. NC_013947.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADD44273; ADD44273; Snas_4630.
GeneID8885835.
KEGGsna:Snas_4630.
PATRIC35371555. VBIStaNas43420_4581.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000242437.
KOK01556.
OMAWGGRLIR.

Enzyme and pathway databases

BioCycSNAS446470:GHHC-4662-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 nameD3Q6N0_STANL
AccessionPrimary (citable) accession number: D3Q6N0
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: February 19, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)