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Q98MD7 (Q98MD7_RHILO) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length415 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

Region128 – 1314Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site1001Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site1011Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2001Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2031Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2251Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2551Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2811Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2261N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
Q98MD7 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 80E85E9CA323E039

FASTA41545,163
        10         20         30         40         50         60 
MRAPLDLAAV EALDAADPLR AMRDRFILPE GVIYLDGNSL GAAAPAVFNE LQKAATQEWA 

        70         80         90        100        110        120 
QDLIRAWNTA SWFDMPVALG DQLGRLIGAV SGQTVVCDTT SINIYKVLHA ALGMRPNRSV 

       130        140        150        160        170        180 
IVAEGDSFPT DLYMAEGVAS TRPGTVLRLE GVDAPTIEEL IDERVAVILV NHVNYKTGQL 

       190        200        210        220        230        240 
RDMAALTCKA HQVGALIVWD LCHTAGALPV ELDAANADFA IGCTYKYLNG GPGAPAFIYA 

       250        260        270        280        290        300 
AKRHHEDVHQ PLSGWWGHAR PFAFEQSYTA GSGIRRFLCG TQPVLSMRAL KGALDIWDDV 

       310        320        330        340        350        360 
DMAAVRKKSI GLTDLFIQLV EARCGAYGLE LEGPRDGNAR GSQVSFLHPH GYQVMRALIE 

       370        380        390        400        410 
RGVIGDFRAP STIRFGFTPL YVGYKDVWQA VEVLEDILRT GAWQEARFAV KTAVT 

« Hide

References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099 EMBL BAB48176.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB48176.1.
RefSeqNP_102390.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98MD7.
SMRQ98MD7. Positions 11-403.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mll0621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB48176; BAB48176; BAB48176.
GeneID1225053.
KEGGmlo:mll0621.
PATRIC22475156. VBIMesLot2464_0498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-502-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 nameQ98MD7_RHILO
AccessionPrimary (citable) accession number: Q98MD7
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2001
Last sequence update: October 1, 2001
Last modified: July 9, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)