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Protein

Kynurenine formamidase

Gene

Afmid

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.UniRule annotation1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.18 mM for N-formyl-L-kynurenine1 Publication
  1. Vmax=42 µmol/min/mg enzyme1 Publication

Pathwayi: L-tryptophan degradation via kynurenine pathway

This protein is involved in step 2 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Tryptophan 2,3-dioxygenase (Tdo2), Indoleamine 2,3-dioxygenase 2 (Ido2), Tryptophan 2,3-dioxygenase (Tdo2), Tryptophan 2,3-dioxygenase (Tdo2)
  2. Kynurenine formamidase (Afmid)
This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621NucleophileCurated
Active sitei247 – 2471Curated
Active sitei279 – 2791Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Tryptophan catabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15003.
BRENDAi3.5.1.9. 3474.
ReactomeiR-MMU-71240. Tryptophan catabolism.
SABIO-RKQ8K4H1.
UniPathwayiUPA00333; UER00454.

Protein family/group databases

ESTHERimouse-KFA. Kynurenine-formamidase.
MEROPSiS09.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynurenine formamidaseUniRule annotation (EC:3.5.1.9UniRule annotation)
Short name:
KFAUniRule annotation
Short name:
KFaseUniRule annotation
Alternative name(s):
ArylformamidaseUniRule annotation
N-formylkynurenine formamidaseUniRule annotation
Short name:
FKFUniRule annotation
Gene namesi
Name:Afmid
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2448704. Afmid.

Subcellular locationi

  • Cytoplasmcytosol UniRule annotation1 Publication
  • Nucleus UniRule annotation1 Publication

  • Note: Predominantly cytosolic. Some fraction is nuclear.

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice display sclerosis of kidney glomeruli, possibly due to failures in the elimination of toxic metabolites.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi162 – 1621S → A: Loss of enzyme activity. 1 Publication
Mutagenesisi247 – 2471D → A: Loss of enzyme activity. 1 Publication
Mutagenesisi279 – 2791H → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 305305Kynurenine formamidasePRO_0000248309Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiQ8K4H1.
PaxDbiQ8K4H1.
PRIDEiQ8K4H1.

PTM databases

iPTMnetiQ8K4H1.
PhosphoSiteiQ8K4H1.

Expressioni

Tissue specificityi

Highly expressed in liver. Expressed in kidney. Weakly or not expressed in other tissues.1 Publication

Inductioni

Down-regulated upon IL2-mediated activation. Transcriptional activation correlates with reduced histone acetylation.1 Publication

Gene expression databases

BgeeiENSMUSG00000017718.
CleanExiMM_AFMID.
ExpressionAtlasiQ8K4H1. baseline and differential.
GenevisibleiQ8K4H1. MM.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ8K4H1. 2 interactions.
MINTiMINT-4117829.
STRINGi10090.ENSMUSP00000073102.

Structurei

3D structure databases

ProteinModelPortaliQ8K4H1.
SMRiQ8K4H1. Positions 15-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi93 – 975HGGXW

Domaini

The main chain amide nitrogen atoms of the second glycine and its adjacent residue in the HGGXW motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.UniRule annotation

Sequence similaritiesi

Belongs to the kynurenine formamidase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG4627. Eukaryota.
COG0657. LUCA.
GeneTreeiENSGT00390000011093.
HOGENOMiHOG000260457.
HOVERGENiHBG100436.
InParanoidiQ8K4H1.
KOiK01432.
PhylomeDBiQ8K4H1.
TreeFamiTF315112.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_03014. KFase. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR027519. KFase_ver/fungi-typ.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K4H1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAFPSLSAGQ NPWRNLSSEE LEKQYSPSRW VIHTKPEEVV GNFVQIGSQA
60 70 80 90 100
TQKARATRRN QLDVPYGDGE GEKLDIYFPD EDSKAFPLFL FLHGGYWQSG
110 120 130 140 150
SKDDSAFMVN PLTAQGIVVV IVAYDIAPKG TLDQMVDQVT RSVVFLQRRY
160 170 180 190 200
PSNEGIYLCG HSAGAHLAAM VLLARWTKHG VTPNLQGFLL VSGIYDLEPL
210 220 230 240 250
IATSQNDPLR MTLEDAQRNS PQRHLDVVPA QPVAPACPVL VLVGQHDSPE
260 270 280 290 300
FHRQSKEFYE TLLRVGWKAS FQQLRGVDHF DIIENLTRED DVLTQIILKT

VFQKL
Length:305
Mass (Da):34,229
Last modified:October 1, 2002 - v1
Checksum:i898000A577132A52
GO
Isoform 2 (identifier: Q8K4H1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     296-305: IILKTVFQKL → VGLTPTTVFL...ITLAGLGLKI

Note: No experimental confirmation available.
Show »
Length:371
Mass (Da):41,574
Checksum:i0F20521893042E06
GO

Sequence cautioni

The sequence AAH24452 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331H → R in AAH43309 (PubMed:15489334).Curated
Sequence conflicti33 – 331H → R in AAH24452 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 30510IILKTVFQKL → VGLTPTTVFLNGQRGSHAHT WAWPGRQEQRERLAVPRWKS QSRLHRRACGECLLFIIVVA ETMSHCITLAGLGLKI in isoform 2. 1 PublicationVSP_020237

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25693.1. [Q8K4H1-1]
RefSeqiNP_082103.1. NM_027827.3. [Q8K4H1-1]
XP_006534309.1. XM_006534246.1. [Q8K4H1-2]
UniGeneiMm.273958.

Genome annotation databases

EnsembliENSMUST00000073388; ENSMUSP00000073102; ENSMUSG00000017718. [Q8K4H1-1]
GeneIDi71562.
KEGGimmu:71562.
UCSCiuc007moa.2. mouse. [Q8K4H1-2]
uc007mob.2. mouse. [Q8K4H1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25693.1. [Q8K4H1-1]
RefSeqiNP_082103.1. NM_027827.3. [Q8K4H1-1]
XP_006534309.1. XM_006534246.1. [Q8K4H1-2]
UniGeneiMm.273958.

3D structure databases

ProteinModelPortaliQ8K4H1.
SMRiQ8K4H1. Positions 15-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K4H1. 2 interactions.
MINTiMINT-4117829.
STRINGi10090.ENSMUSP00000073102.

Protein family/group databases

ESTHERimouse-KFA. Kynurenine-formamidase.
MEROPSiS09.977.

PTM databases

iPTMnetiQ8K4H1.
PhosphoSiteiQ8K4H1.

Proteomic databases

MaxQBiQ8K4H1.
PaxDbiQ8K4H1.
PRIDEiQ8K4H1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073388; ENSMUSP00000073102; ENSMUSG00000017718. [Q8K4H1-1]
GeneIDi71562.
KEGGimmu:71562.
UCSCiuc007moa.2. mouse. [Q8K4H1-2]
uc007mob.2. mouse. [Q8K4H1-1]

Organism-specific databases

CTDi125061.
MGIiMGI:2448704. Afmid.

Phylogenomic databases

eggNOGiKOG4627. Eukaryota.
COG0657. LUCA.
GeneTreeiENSGT00390000011093.
HOGENOMiHOG000260457.
HOVERGENiHBG100436.
InParanoidiQ8K4H1.
KOiK01432.
PhylomeDBiQ8K4H1.
TreeFamiTF315112.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00454.
BioCyciMetaCyc:MONOMER-15003.
BRENDAi3.5.1.9. 3474.
ReactomeiR-MMU-71240. Tryptophan catabolism.
SABIO-RKQ8K4H1.

Miscellaneous databases

PROiQ8K4H1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000017718.
CleanExiMM_AFMID.
ExpressionAtlasiQ8K4H1. baseline and differential.
GenevisibleiQ8K4H1. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_03014. KFase. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR027519. KFase_ver/fungi-typ.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKFA_MOUSE
AccessioniPrimary (citable) accession number: Q8K4H1
Secondary accession number(s): B1AQK9, Q80XP3, Q8R1K6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2002
Last modified: September 7, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.