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C3LGW9 (C3LGW9_BACAC) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 40. 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

Names and origin

Protein namesRecommended name:
Kynureninase PIRNR PIRNR038800 HAMAP-Rule MF_01970

EC=3.7.1.3 PIRNR PIRNR038800 HAMAP-Rule MF_01970
Alternative name(s):
L-kynurenine hydrolase HAMAP-Rule MF_01970
Gene names
Name:kynU HAMAP-Rule MF_01970 EMBL ACP15882.1
Ordered Locus Names:BAMEG_1842 EMBL ACP15882.1
OrganismBacillus anthracis (strain CDC 684 / NRRL 3495) [Complete proteome] [HAMAP] EMBL ACP15882.1
Taxonomic identifier568206 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length428 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

Region132 – 1354Pyridoxal 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 site2131Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2161Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2381Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2671Pyridoxal phosphate By similarity HAMAP-Rule MF_01970
Binding site2951Pyridoxal phosphate By similarity HAMAP-Rule MF_01970

Amino acid modifications

Modified residue2391N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01970

Sequences

Sequence LengthMass (Da)Tools
C3LGW9 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: B9E54DCE8E5CA643

FASTA42848,602
        10         20         30         40         50         60 
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS 

        70         80         90        100        110        120 
WKEYGIDGWT EGEHPWFFLS EKLGELTAPL IGALPEETIV TGSTTTNIHQ VIATFYEPKG 

       130        140        150        160        170        180 
IRTKILADEL TFPSDIYALQ SQIRLKGLDP DEHLVRVKSR DGRTLSEDDI IQAMTDDIAL 

       190        200        210        220        230        240 
ILLPSVLYRS GQILDMKRLT AEAHERGIHI GFDLCHSIGS IPHHFKEWDV DFAIWCNYKY 

       250        260        270        280        290        300 
LNAGPGGVAG LYVNKKHFNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS 

       310        320        330        340        350        360 
TAPLIGSLEI FKEAGIERLR EKSLHITRFM LNLIAHELSD FGFTIGNPLE DEKRGGHIYL 

       370        380        390        400        410        420 
EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWQSVMILKK IMKDEEYKQF 


ENKREVVA 

« Hide

References

[1]"Genome sequence of Bacillus anthracis str. CDC 684."
Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C., Sutton G., Sims D.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 684 / NRRL 3495.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001215 Genomic DNA. Translation: ACP15882.1.
RefSeqYP_002814443.1. NC_012581.1.

3D structure databases

ProteinModelPortalC3LGW9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING568206.BAMEG_1842.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP15882; ACP15882; BAMEG_1842.
GeneID7786306.
KEGGbah:BAMEG_1842.
PATRIC18793440. VBIBacAnt127120_2098.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3844.
HOGENOMHOG000242438.
KOK01556.
OMAHVAYRSA.
OrthoDBEOG6N67XP.

Enzyme and pathway databases

BioCycBANT568206:GHVT-1812-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 nameC3LGW9_BACAC
AccessionPrimary (citable) accession number: C3LGW9
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: July 9, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)