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B5XB27 (AFMID_SALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 16. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable arylformamidase

EC=3.5.1.9
Alternative name(s):
Kynurenine formamidase
Short name=KF
Gene names
Name:afmid
OrganismSalmo salar (Atlantic salmon)
Taxonomic identifier8030 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiProtacanthopterygiiSalmoniformesSalmonidaeSalmoninaeSalmo

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites By similarity.

Catalytic activity

N-formyl-L-kynurenine + H2O = formate + L-kynurenine.

Pathway

Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 2/2.

Subcellular location

Cytoplasmcytosol By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the AFMID family.

Ontologies

Keywords
   Biological processTryptophan catabolism
   Cellular componentCytoplasm
Nucleus
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processtryptophan catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarylformamidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Probable arylformamidase
PRO_0000361879

Sites

Active site1531 By similarity
Active site2361 By similarity
Active site2691 By similarity

Sequences

Sequence LengthMass (Da)Tools
B5XB27 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 8ABC38B02E85DF67

FASTA29432,682
        10         20         30         40         50         60 
MSRWKDMNKD ELERQFSPSQ WSHRMSADDV IKSHVTALKE GTERARGLAQ TLLNVPYGEG 

        70         80         90        100        110        120 
EGEKLDVYVP TTTSLDVPLV IYLHGGYWQF LSKEESGFMA VPLVHKGVVV VAVGYDIAPK 

       130        140        150        160        170        180 
GNMDVMVSQV RRSVVSVIQQ YSHISGLYLC GHSAGAHLAA MILSTDWSQY SVTPQIKGAF 

       190        200        210        220        230        240 
LVSGIYDLLP ILSTYVNEPL KMTEEVALRN SPSQLVPQLK LSSSNCDIVV AVAQNDSPEF 

       250        260        270        280        290 
RKQSEDYYKA LESTEGLKVT LEDVPNTDHF NIIEQLVDGD YHLTQLLLKM MGKS 

« Hide

References

[1]"Salmo salar and Esox lucius full-length cDNA sequences reveal changes in evolutionary pressures on a post-tetraploidization genome."
Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M., Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S., Koop B.F.
BMC Genomics 11:279-279(2010) [PubMed: 20433749] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT048246 mRNA. Translation: ACI68047.1.
RefSeqNP_001134570.1. NM_001141098.2.
UniGeneSsa.2978.

3D structure databases

ProteinModelPortalB5XB27.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100196069.

Organism-specific databases

CTD125061.

Phylogenomic databases

HOVERGENHBG100436.

Family and domain databases

InterProIPR013094. AB_hydrolase_3.
[Graphical view]
PfamPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAFMID_SALSA
AccessionPrimary (citable) accession number: B5XB27
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 25, 2008
Last modified: June 28, 2011
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families