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B6IV21 (B6IV21_RHOCS) 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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Names and origin

Protein attributes

Sequence length412 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

Region126 – 1294Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01970

Sites

Binding site981Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_01970
Binding site991Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1681Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site1971Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2001Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2221Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2521Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2781Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2231N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
B6IV21 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: BB5B5D213F424173

FASTA41244,151
        10         20         30         40         50         60 
MTLGRADLEA LDAADPLAPF RDEFALPEGV LYLDGNSLGA LPRATPARLA RLVQEEWGRD 

        70         80         90        100        110        120 
LIRSWNTAGW IDLPRRVGEA IAPVVGAGPG QVIAADSTSV NLFKLAAAAV GMRPGRRVIL 

       130        140        150        160        170        180 
SEPGNFPTDL YVLQGLAELL GDRVELVLAE RHELADALDG DVALLLLTHV HYKTGRVHDL 

       190        200        210        220        230        240 
PGLTAAAHAA GALTLWDLSH SAGALEVGLD AAGADFAVGC GYKYLNGGPG APAWLYVAQR 

       250        260        270        280        290        300 
HQDQVRPPLA GWMGHAAPFA FEDRFRPADG MARQLCGTPG ILGMAALEEG VRIVARADRA 

       310        320        330        340        350        360 
RLREKSRRMG DLFLALVAEQ CGPDTFALAC PADGAERGSQ VSLSHPEGYA IIQALIARGV 

       370        380        390        400        410 
IGDFRAPDIL RFGFAPLYLR YTDIWDAVVH LAAVMRDGEW QADRFRQRAA VT 

« Hide

References

[1]"Genome sequence of Rhodospirillum centenum."
Touchman J.W., Bauer C., Blankenship R.E.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51521 / SW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000613 Genomic DNA. Translation: ACJ00145.1.
RefSeqYP_002298957.1. NC_011420.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING414684.RC1_2772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ00145; ACJ00145; RC1_2772.
GeneID7007540.
KEGGrce:RC1_2772.
PATRIC23320732. VBIRhoCen1465_2689.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242437.
KOK01556.
OMAVWDLAHS.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycRCEN414684:GHCM-2750-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 nameB6IV21_RHOCS
AccessionPrimary (citable) accession number: B6IV21
Entry history
Integrated into UniProtKB/TrEMBL: December 16, 2008
Last sequence update: December 16, 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)