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E2RB73 (E2RB73_CANFA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 31. Feed History...

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

Sequence length464 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

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. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity By similarity. HAMAP-Rule MF_03017

Catalytic activity

L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_03017

L-kynurenine + H2O = anthranilate + L-alanine. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Cofactor

Pyridoxal phosphate By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Pathway

Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Subunit structure

Homodimer By similarity. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Subcellular location

Cytoplasm By similarity PIRNR PIRNR038800 HAMAP-Rule MF_03017.

Sequence similarities

Belongs to the kynureninase family. PIRNR PIRNR038800 HAMAP-Rule MF_03017

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data. Ensembl ENSCAFP00000008166

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis PIRNR PIRNR038800 HAMAP-Rule MF_03017
   Cellular componentCytoplasm PIRNR PIRNR038800 HAMAP-Rule MF_03017
   LigandPyridoxal phosphate PIRNR PIRNR038800 HAMAP-Rule MF_03017
   Molecular functionHydrolase PIRNR PIRNR038800 HAMAP-Rule MF_03017
   PTMAcetylation HAMAP-Rule MF_03017
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' NAD biosynthetic process from tryptophan

Inferred from electronic annotation. Source: UniProtKB-HAMAP

L-kynurenine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

anthranilate metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

quinolinate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

response to vitamin B6

Inferred from electronic annotation. Source: Ensembl

tryptophan catabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionkynureninase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region165 – 1684Pyridoxal phosphate binding By similarity HAMAP-Rule MF_03017

Sites

Binding site1371Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_03017
Binding site1381Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2501Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2531Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2751Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site3051Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site3331Pyridoxal phosphate By similarity HAMAP-Rule MF_03017

Amino acid modifications

Modified residue11N-acetylmethionine By similarity HAMAP-Rule MF_03017
Modified residue2761N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_03017

Sequences

Sequence LengthMass (Da)Tools
E2RB73 [UniParc].

Last modified October 31, 2012. Version 2.
Checksum: 48064619A1E32286

FASTA46452,514
        10         20         30         40         50         60 
MEPLPLELPA DTVQRIASEL RCHPTDERVA LRLDEEDKLR HFKEHFHIPK MQDLPAIDLS 

        70         80         90        100        110        120 
LVNKDENAIY FSGNSLGLQP KLVKTYLEEE LDKWAKMGVY GHEVGKRPWI TGDETILGLM 

       130        140        150        160        170        180 
NDIVGANEKE IALMNGLTVN LHLLLLSFFK PTPERYKILL EAKAFPSDHY VIESQLQLHG 

       190        200        210        220        230        240 
LNVEKSMRII KPREGEETLR TEDILEVIEK EGDSIAVILF GGLHFYTGQL FNIPAITRAG 

       250        260        270        280        290        300 
QAKGCFVGFD LAHAVGNVEL HLHDWGVDFA CWCSYKYLNS GAGGLAGAFV HEKHAYRIKP 

       310        320        330        340        350        360 
ALVGWFGHEL SSRFKMDNKL QLSPGVSGFR ISNPPILLVC SLQASLEIFK QATMKALRRK 

       370        380        390        400        410        420 
SILLTGYLEY LIKHYYNKDT ADTKKPFVNI ITPSCIEERG CQLTLTFSVP MKYVFQELEK 

       430        440        450        460 
RGVVCDKREP NGIRVAPVPL YNSFHDVYKF INLLTSTLDS AETK 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence, comparative analysis and haplotype structure of the domestic dog."
Broad Sequencing Platform
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R. expand/collapse author list , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Boxer Ensembl ENSCAFP00000008166.
[2]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.
Strain: Boxer Ensembl ENSCAFP00000008166.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAEX03011933 Genomic DNA. No translation available.
RefSeqXP_005632015.1. XM_005631958.1.
XP_005632016.1. XM_005631959.1.
XP_541027.3. XM_541027.4.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000008804; ENSCAFP00000008166; ENSCAFG00000005466.
GeneID483907.
KEGGcfa:483907.

Organism-specific databases

CTD8942.

Phylogenomic databases

GeneTreeENSGT00390000008033.
KOK01556.
OMAGLMNDIV.
OrthoDBEOG7D2FDV.
TreeFamTF300707.

Enzyme and pathway databases

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 nameE2RB73_CANFA
AccessionPrimary (citable) accession number: E2RB73
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: October 31, 2012
Last modified: July 9, 2014
This is version 31 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)