Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8K4H1 (AFMID_MOUSE)

Last modified February 9, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length305 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.1

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. Nucleus. Note: Predominantly cytosolic. Some fraction is nuclear. Ref.2

Tissue specificity

Highly expressed in liver. Expressed in kidney. Weakly or not expressed in other tissues. Ref.2

Induction

Down-regulated upon IL2-mediated activation. Transcriptional activation correlates with reduced histone acetylation. Ref.2

Post-translational modification

The N-terminus is blocked.

Disruption phenotype

Mice display sclerosis of kidney glomeruli, possibly due to failures in the elimination of toxic metabolites. Ref.5

Miscellaneous

The Afmid gene shares a bidirectional promoter region with Tk1 gene.

Sequence similarities

Belongs to the AFMID family.

Biophysicochemical properties

Kinetic parameters:

KM=0.18 mM for N-formyl-L-kynurenine

Vmax=42 µmol/min/mg enzyme

Ontologies

Keywords
   Biological processTryptophan catabolism
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processtryptophan catabolic process to kynurenine Ref.5

Inferred from direct assay. Source: MGI

   Cellular componentcytosol Ref.1

Inferred from Experiment. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarylformamidase activity Ref.1

Inferred from Experiment. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K4H1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8K4H1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     296-305: IILKTVFQKL → VGLTPTTVFL...ITLAGLGLKI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 305305Probable arylformamidase
PRO_0000248309

Sites

Active site1621 Probable
Active site2471 Probable
Active site2791 Probable

Natural variations

Alternative sequence296 – 30510IILKTVFQKL → VGLTPTTVFLNGQRGSHAHT WAWPGRQEQRERLAVPRWKS QSRLHRRACGECLLFIIVVA ETMSHCITLAGLGLKI in isoform 2.
VSP_020237

Experimental info

Mutagenesis1621S → A: Loss of enzyme activity. Ref.6
Mutagenesis2471D → A: Loss of enzyme activity. Ref.6
Mutagenesis2791H → A: Loss of enzyme activity. Ref.6
Sequence conflict331H → R in AAH43309. Ref.4
Sequence conflict331H → R in AAH24452. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 898000A577132A52

FASTA30534,229
        10         20         30         40         50         60 
MAFPSLSAGQ NPWRNLSSEE LEKQYSPSRW VIHTKPEEVV GNFVQIGSQA TQKARATRRN 

        70         80         90        100        110        120 
QLDVPYGDGE GEKLDIYFPD EDSKAFPLFL FLHGGYWQSG SKDDSAFMVN PLTAQGIVVV 

       130        140        150        160        170        180 
IVAYDIAPKG TLDQMVDQVT RSVVFLQRRY PSNEGIYLCG HSAGAHLAAM VLLARWTKHG 

       190        200        210        220        230        240 
VTPNLQGFLL VSGIYDLEPL IATSQNDPLR MTLEDAQRNS PQRHLDVVPA QPVAPACPVL 

       250        260        270        280        290        300 
VLVGQHDSPE FHRQSKEFYE TLLRVGWKAS FQQLRGVDHF DIIENLTRED DVLTQIILKT 


VFQKL 

« Hide

Isoform 2.

Checksum: 0F20521893042E06
Show »

FASTA37141,574

References

« Hide 'large scale' references
[1]"Kynurenine formamidase: determination of primary structure and modeling-based prediction of tertiary structure and catalytic triad."
Pabarcus M.K., Casida J.E.
Biochim. Biophys. Acta 1596:201-211(2002) [PubMed: 12007602] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 16-29; 35-53; 150-160 AND 224-242, FUNCTION.
Strain: Swiss Webster.
Tissue: Liver.
[2]"Alternate activation of two divergently transcribed mouse genes from a bidirectional promoter is linked to changes in histone modification."
Schuettengruber B., Doetzlhofer A., Kroboth K., Wintersberger E., Seiser C.
J. Biol. Chem. 278:1784-1793(2003) [PubMed: 12411446] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Kidney and Liver.
[5]"Effect of arylformamidase (kynurenine formamidase) gene inactivation in mice on enzymatic activity, kynurenine pathway metabolites and phenotype."
Dobrovolsky V.N., Bowyer J.F., Pabarcus M.K., Heflich R.H., Williams L.D., Doerge D.R., Arvidsson B., Bergquist J., Casida J.E.
Biochim. Biophys. Acta 1724:163-172(2005) [PubMed: 15866519] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[6]"Cloning, expression, and catalytic triad of recombinant arylformamidase."
Pabarcus M.K., Casida J.E.
Protein Expr. Purif. 44:39-44(2005) [PubMed: 15935693] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-162; ASP-247 AND HIS-279.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF399717 mRNA. Translation: AAM62284.1.
AY099479 mRNA. Translation: AAM44406.1.
AL591433 Genomic DNA. Translation: CAM19096.1.
BC024452 mRNA. Translation: AAH24452.1. Different initiation.
BC043309 mRNA. Translation: AAH43309.1.
BC066780 mRNA. Translation: AAH66780.1.
IPIIPI00281894.
IPI00649750.
RefSeqNP_082103.1.
UniGeneMm.273958

3D structure databases

SMRQ8K4H1. Positions 19-298.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8K4H1.

Protein family/group databases

MEROPSS09.977.

Proteomic databases

PRIDEQ8K4H1.

Genome annotation databases

EnsemblENSMUST00000073388; ENSMUSP00000073102; ENSMUSG00000017718; Mus musculus. [Genome view]
GeneID71562.
KEGGmmu:71562.
NMPDRfig|10090.3.peg.25709.
UCSCuc007moa.1. mouse.
uc007mob.1. mouse.

Organism-specific databases

CTD71562.
MGIMGI:2448704. Afmid.

Phylogenomic databases

eggNOGroNOG15097.
HOVERGENQ8K4H1.
InParanoidQ8K4H1.
OMAMVLSTDW.
OrthoDBEOG9FN743.
PhylomeDBQ8K4H1.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15003.
BRENDA3.5.1.9. 244.

Gene expression databases

ArrayExpressQ8K4H1.
BgeeQ8K4H1.
CleanExMM_AFMID.
GenevestigatorQ8K4H1.
GermOnlineENSMUSG00000017718. Mus musculus.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio334001.
SOURCESearch...

Entry information

Entry nameAFMID_MOUSE
AccessionPrimary (citable) accession number: Q8K4H1
Secondary accession number(s): B1AQK9, Q80XP3, Q8R1K6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2002
Last modified: February 9, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents