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Q5DGJ1

- KYNU_SCHJA

UniProt

Q5DGJ1 - KYNU_SCHJA

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Protein

Kynureninase

Gene

SJCHGC00887

Organism
Schistosoma japonicum (Blood fluke)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

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

Cofactori

Pyridoxal phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei88 – 881Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei89 – 891Pyridoxal phosphateUniRule annotation
Binding sitei202 – 2021Pyridoxal phosphateUniRule annotation
Binding sitei205 – 2051Pyridoxal phosphateUniRule annotation
Binding sitei227 – 2271Pyridoxal phosphateUniRule annotation
Binding sitei280 – 2801Pyridoxal phosphateUniRule annotation
Binding sitei308 – 3081Pyridoxal 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

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

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
ORF Names:SJCHGC00887
OrganismiSchistosoma japonicum (Blood fluke)
Taxonomic identifieri6182 [NCBI]
Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436KynureninasePRO_0000356960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei228 – 2281N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi6182.Q5DGJ1.

Structurei

3D structure databases

ProteinModelPortaliQ5DGJ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 1194Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.

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.

Q5DGJ1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKILQYKSIE NVQYSKNILY FCGHSMGLQP KSTKIYINKI LNQWKNLGVL
60 70 80 90 100
SYHYGELPAS YCDEQLSIDC AQWIVNAKFN EVSITCNLTV NMHVLIAKFY
110 120 130 140 150
RPTNEKYCIL IENDIFPSDY YVLESHIQWH GYNTNDCFIK LKPRLHEYCL
160 170 180 190 200
RNDDILPEII KNQHRIALIW LPGIQYITGQ LFNMKLITEW GHQYAKCPVG
210 220 230 240 250
WDLAHAVGNI PLYLHDWNID MAVWCSYKYL NGSPGAIGGL FIHEKHHHEE
260 270 280 290 300
GSYGPKFIEF TNNNNITIFN NINGPQLTGW WSHRSETRFN MTGNMELAKG
310 320 330 340 350
ANAYRLSNPP LLLAAALTVS VNIIKSCGGM INLREKSIKL TDYLEYLITN
360 370 380 390 400
SSLALKHDHY CLVTPSNSNE RGAQLTISVT HMNIQVVYEN LLKLGVICDY
410 420 430
RLPNFLRITP IPLYNSFEDV YLLAKCLHQV LNDTLN
Length:436
Mass (Da):50,248
Last modified:March 29, 2005 - v1
Checksum:iD2585D22865EC083
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY813333 mRNA. Translation: AAW25065.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY813333 mRNA. Translation: AAW25065.1 .

3D structure databases

ProteinModelPortali Q5DGJ1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6182.Q5DGJ1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3844.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .

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

  1. "New perspectives on host-parasite interplay by comparative transcriptomic and proteomic analyses of Schistosoma japonicum."
    Liu F., Lu J., Hu W., Wang S.-Y., Cui S.-J., Chi M., Yan Q., Wang X.-R., Song H.-D., Xu X.-N., Wang J.-J., Zhang X.-L., Zhang X., Wang Z.-Q., Xue C.-L., Brindley P.J., McManus D.P., Yang P.-Y.
    , Feng Z., Chen Z., Han Z.-G.
    PLoS Pathog. 2:268-281(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiKYNU_SCHJA
AccessioniPrimary (citable) accession number: Q5DGJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 29, 2005
Last modified: October 29, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3