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F7VS63 (F7VS63_SORMK) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 21. 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 length495 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_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 EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL CCC08349.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region185 – 1884Pyridoxal phosphate binding By similarity HAMAP-Rule MF_03017

Sites

Binding site1561Pyridoxal phosphate; via amide nitrogen By similarity HAMAP-Rule MF_03017
Binding site1571Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2701Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2731Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site2951Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site3371Pyridoxal phosphate By similarity HAMAP-Rule MF_03017
Binding site3651Pyridoxal phosphate By similarity HAMAP-Rule MF_03017

Amino acid modifications

Modified residue2961N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_03017

Sequences

Sequence LengthMass (Da)Tools
F7VS63 [UniParc].

Last modified September 21, 2011. Version 1.
Checksum: 76235340CF95BE8C

FASTA49554,196
        10         20         30         40         50         60 
MTASSWPTNN DNHPTNSPAK WKNMSTAAVQ DARKQAEALD NEDPIAFIRD EFNIPTKAQI 

        70         80         90        100        110        120 
ASSRLADSHP AALPASKDDA KSVYLCGNSL GVQPKRTVTR LNQYLTTWAT QGVQGHFKPL 

       130        140        150        160        170        180 
EESPLPTWLD ADAKAAELIA PVVGADVSEV AVMQTLTANI HLLMSAFYRP DINNRHKVIL 

       190        200        210        220        230        240 
ENKAFPSDHF VVETQIRHHS LSTEKSMVLI DSSSKDNIIT TQEILSVISA HADTTALLLL 

       250        260        270        280        290        300 
PGIQYYTGQL LDIPAITAFA HKHGIFVIWD LAHAVGNVPL YLHDWGVDAA AWCSYKYLNG 

       310        320        330        340        350        360 
GPGCIGGLFV HTNNSIVTKE ITDEKPEEGY SNRLAGWWGN DKKTRFVMAN KFHPVAGAAG 

       370        380        390        400        410        420 
FQLSNPSILD ITSLSASLEI FQEAGGMEAL RSKSLKLTNF LEATLGGMKE EDRAHFRIIT 

       430        440        450        460        470        480 
PSKPEERGAQ LSLMLSDGLL DTVMKELEAR GVIVDERRPN VIRVAPAPLY NTFSDCVQFV 

       490 
EAFSAALEAA TKRAL 

« Hide

References

[1]"De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis."
Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K., Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D., Poeggeler S., Read N., Seiler S., Smith K., Zickler D., Kueck U., Freitag M.
PLoS Genet. 6:E1000891-E1000891(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell.
Tissue: Mycelium EMBL CCC08349.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CABT02000005 Genomic DNA. Translation: CCC08349.1.
RefSeqXP_003348873.1. XM_003348825.1.

3D structure databases

ProteinModelPortalF7VS63.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10806334.
KEGGsmp:SMAC_01897.

Phylogenomic databases

KOK01556.
OrthoDBEOG7V1G0J.

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 nameF7VS63_SORMK
AccessionPrimary (citable) accession number: F7VS63
Entry history
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: July 9, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)