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

H2K945 (H2K945_STRHJ) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 15. 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 length403 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

Region135 – 1384Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1061Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1071Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2041Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2071Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2291Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2591Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2851Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2301N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
H2K945 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: 042DCE3677FACBE7

FASTA40343,016
        10         20         30         40         50         60 
MSELPLLAKE LDQADELAPL RDRFVLDSAS GDAAGPAGVY LDGNSLGALP AHVPDRVADV 

        70         80         90        100        110        120 
VRRQWGELRI RSWEESGWWT APERIGDRIA PLVGAAPGQI VVGDSTSVNV FKALVAAIRM 

       130        140        150        160        170        180 
ADAGRDEILV DATTFPTDGY IAESAARLTG RTLRAVTPAE VPAALGDRTA AVLLNHVDYR 

       190        200        210        220        230        240 
TGRLHDLPAL TAAVHACGAL AVWDLCHSAG ALPVGLDEHG VDLAVGCTYK YLNGGPGSPA 

       250        260        270        280        290        300 
YLYVRRELQD RFDSPLPGWN SHAEPFGMSP SYAPAAGAVR GRVGTPDILS LLALEAALDV 

       310        320        330        340        350        360 
WDGVSVDAVR AKSLALTDFF LRCVDEYTEP GRVECVTPGP HAERGSQIAL RCPDAGEVMK 

       370        380        390        400 
RLIARGVVGD FRHPDILRFG FTPLYVSFRD AERAARTLGE ELA 

« Hide

References

[1]"Genomic analysis of Streptomyces hygroscopicus subsp. jinggangensis 5008."
Wu H., Bai L.
Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5008.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003275 Genomic DNA. Translation: AEY90659.1.
RefSeqYP_006246532.1. NC_017765.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEY90659; AEY90659; SHJG_5391.
GeneID12810804.
KEGGshy:SHJG_5391.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

BioCycSHYG1133850:GLLU-5437-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 nameH2K945_STRHJ
AccessionPrimary (citable) accession number: H2K945
Entry history
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: February 19, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)