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B1VMD2 (B1VMD2_STRGG) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 39. Feed History...

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

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Region133 – 1364Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1041Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1051Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2021Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2051Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2271Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2571Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2831Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2281N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
B1VMD2 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 795BDBD4DE73799C

FASTA41043,258
        10         20         30         40         50         60 
MSETTTTARD LRERAAVLDA ADPLAARREL FALDDGVYLD GNSLGALPVH VPARVQDVLT 

        70         80         90        100        110        120 
RQWGQLRIRS WDESGWWTAP ERIGDRIAPL VGAAAGQIVV GDSTSVNVFK AVVAAGRLAG 

       130        140        150        160        170        180 
EGRDEILVDA TTFPTDGYIA SAAARLTGHR IVPVAPADVP AALGPRTAAV LLNHVDYRSG 

       190        200        210        220        230        240 
RLHDLPGLTA AVHAAGAVVV WDLCHSAGAL PVGLDEHRVD LAVGCTYKYL NGGPGSPAYL 

       250        260        270        280        290        300 
YVAERHQAAF DSPLPGWNSH ADPFGMTSGY APADGSVRGR VGTPDIVSML TLEAALDVWD 

       310        320        330        340        350        360 
GVPVDAVRAK SLALTDFFLE CVEAYVPAGR VTSVTPAAHA ERGSQVALRC AEAEPVMRRL 

       370        380        390        400        410 
IERGVVGDLR RPDVLRFGFT PLYVGFADAE RAARILAEVL AEVSAGDTVG 

« Hide

References

[1]"Genome sequence of the streptomycin-producing microorganism Streptomyces griseus IFO 13350."
Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H., Yamashita A., Hattori M., Horinouchi S.
J. Bacteriol. 190:4050-4060(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 4626 / NBRC 13350.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009493 Genomic DNA. Translation: BAG20242.1.
RefSeqYP_001824925.1. NC_010572.1.

3D structure databases

ProteinModelPortalB1VMD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING455632.SGR_3413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG20242; BAG20242; SGR_3413.
GeneID6214162.
KEGGsgr:SGR_3413.
PATRIC23753396. VBIStrGri32265_3487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAYLATWRT.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycSGRI455632:GD3A-3436-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 nameB1VMD2_STRGG
AccessionPrimary (citable) accession number: B1VMD2
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: July 9, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)