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I0JSH9 (I0JSH9_HALH3) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 16. Feed History...

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

Sequence length426 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 site1021Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1031Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2111Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2141Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2361Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2651Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2931Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2371N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
I0JSH9 [UniParc].

Last modified June 13, 2012. Version 1.
Checksum: 3281C3699AF84B54

FASTA42647,758
        10         20         30         40         50         60 
MTKPKITLET AAKLDQKDVL HNFKKEFYTD DNRFYMDGNS LGLLSKRAEQ SLLSSLEDWK 

        70         80         90        100        110        120 
THAIGGWTDG KEPWFYMSEK FGAKTAPLLG AKPEEVISTG SITSNLHQLL STFYRPEGQR 

       130        140        150        160        170        180 
TKILADELNF PSDIYALKSQ LELHGMDPDE HLIQVKSDNG ATLSEEDIIK EMRSDIALLL 

       190        200        210        220        230        240 
LPSVLYRSGQ LLDIEKITKA AHEQGIMVGF DLAHSIGALP HNLDDWGVDF AVWCTYKYLN 

       250        260        270        280        290        300 
SGPGGVGGLY VNEKHLGSKP GLAGWFSSKK DKQFDMAHDL NHAETAGAYQ MGTPHILSSA 

       310        320        330        340        350        360 
PLLGSLDLFQ EADIKNVRCK SLQMTRLMLD LVYQELDGLG FQIITPLEDE RRGGHISLVH 

       370        380        390        400        410        420 
SEAASICKAL KKENVVPDFR APDVIRLAPV ALYTTYKEVY EVMMILKEIM VNETYKKYKN 


ERDIIA 

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References

[1]"Chloride and organic osmolytes: a hybrid strategy to cope with elevated salinities by the moderately halophilic, chloride-dependent bacterium Halobacillus halophilus."
Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V., Oesterhelt D.
Environ. Microbiol. 15:1619-1633(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35676 / DSM 2266 / JCM 20832 / NBRC 102448/ NCIMB 2269.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE717023 Genomic DNA. Translation: CCG47101.1.
RefSeqYP_006182372.1. NC_017668.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCG47101; CCG47101; HBHAL_4763.
GeneID12746449.
KEGGhhd:HBHAL_4763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01556.

Enzyme and pathway databases

BioCycHHAL866895:GLDT-3800-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 nameI0JSH9_HALH3
AccessionPrimary (citable) accession number: I0JSH9
Entry history
Integrated into UniProtKB/TrEMBL: June 13, 2012
Last sequence update: June 13, 2012
Last modified: February 19, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)