Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

F8JVJ1

- F8JVJ1_STREN

UniProt

F8JVJ1 - F8JVJ1_STREN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Kynureninase

Gene

kynU

Organism
Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation
L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation

Cofactori

Note: Pyridoxal phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei107 – 1071Pyridoxal phosphateUniRule annotation
Binding sitei204 – 2041Pyridoxal phosphateUniRule annotation
Binding sitei207 – 2071Pyridoxal phosphateUniRule annotation
Binding sitei229 – 2291Pyridoxal phosphateUniRule annotation
Binding sitei259 – 2591Pyridoxal phosphateUniRule annotation
Binding sitei285 – 2851Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Biological processi

Pyridine nucleotide biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciSCAT1003195:GJCM-3349-MONOMER.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynUUniRule annotationImported
Ordered Locus Names:SCAT_3326Imported, SCATT_33190Imported
OrganismiStreptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057)Imported
Taxonomic identifieri1003195 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
ProteomesiUP000007842: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1384Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

KOiK01556.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

F8JVJ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSETTTPATA AALDDRAAAL DAADPLAALR ERFVLDDTVY LDGNSLGALP
60 70 80 90 100
KNVAGRLAEV VEDEWGRLRI RSWDESGWWT APERVGERIA PLVGAAPGQI
110 120 130 140 150
VVGDSTSVNV FKAVVAATRL AGPGRDEVLV DAATFPTDGY VAASAARLTG
160 170 180 190 200
HTVRPVAAGE MAAAAGARTA ALLVNHVDYR TGELADLPGI TAAAHAAGAV
210 220 230 240 250
AVWDLCHSAG ALPVGLDEHG VDLAVGCTYK YLNGGPGAPA FLYLARRIQD
260 270 280 290 300
RFDSPLPGWN SHTDPFAMRP GYEAAPGAVR GRVGTPEILS LLALEAALEV
310 320 330 340 350
WEGVDVAQVR AKSLALTDFF LECVAALVPD GRLEPVTPAE HARRGSQVSL
360 370 380 390 400
RCADAGAVMA ALIERGVVGD FRRPDVLRFG FTPLYTGFAD VLRAARVLAD

TVR
Length:403
Mass (Da):42,215
Last modified:September 21, 2011 - v1
Checksum:iB3E49DBE3FC3CBFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003219 Genomic DNA. Translation: AEW95690.1.
FQ859185 Genomic DNA. Translation: CCB76028.1.
RefSeqiYP_004912833.1. NC_016111.1.
YP_006055212.1. NC_017586.1.

Genome annotation databases

EnsemblBacteriaiAEW95690; AEW95690; SCATT_33190.
CCB76028; CCB76028; SCAT_3326.
GeneIDi11358482.
12650089.
KEGGisct:SCAT_3326.
scy:SCATT_33190.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003219 Genomic DNA. Translation: AEW95690.1 .
FQ859185 Genomic DNA. Translation: CCB76028.1 .
RefSeqi YP_004912833.1. NC_016111.1.
YP_006055212.1. NC_017586.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEW95690 ; AEW95690 ; SCATT_33190 .
CCB76028 ; CCB76028 ; SCAT_3326 .
GeneIDi 11358482.
12650089.
KEGGi sct:SCAT_3326.
scy:SCATT_33190.

Phylogenomic databases

KOi K01556.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .
BioCyci SCAT1003195:GJCM-3349-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_01970. Kynureninase.
InterProi IPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR14084. PTHR14084. 1 hit.
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF038800. KYNU. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01814. kynureninase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Streptomyces cattleya NRRL 8057, a producer of antibiotics and fluorometabolites."
    Barbe V., Bouzon M., Mangenot S., Badet B., Poulain J., Segurens B., Vallenet D., Marliere P., Weissenbach J.
    J. Bacteriol. 193:5055-5056(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NRRL 8057Imported.
  2. Genoscope - CEA
    Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: NRRL 8057Imported.
  3. "Complete genome sequence of Streptomyces cattleya strain DSM 46488."
    Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.
    Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057Imported.
  4. Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.
    Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 46488Imported.

Entry informationi

Entry nameiF8JVJ1_STREN
AccessioniPrimary (citable) accession number: F8JVJ1
Secondary accession number(s): G8WQT1
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: November 26, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3