Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Kynurenine formamidase

Gene

kynB

Organism
Salinibacter ruber (strain DSM 13855 / M31)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation.UniRule annotation

Catalytic activityi

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

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. no protein annotated in this organism
  2. Kynurenine formamidase (kynB)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Tryptophan catabolism

Enzyme and pathway databases

BioCyciSRUB309807:GJJD-1500-MONOMER.
UniPathwayiUPA00333; UER00454.

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:kynBUniRule annotation
Ordered Locus Names:SRU_1503
OrganismiSalinibacter ruber (strain DSM 13855 / M31)
Taxonomic identifieri309807 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter
Proteomesi
  • UP000008674 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Kynurenine formamidasePRO_0000362138Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi309807.SRU_1503.

Structurei

3D structure databases

ProteinModelPortaliQ2S2F5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the KynB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107XCH. Bacteria.
COG1878. LUCA.
HOGENOMiHOG000219455.
KOiK07130.
OMAiMDAHHRI.
OrthoDBiPOG091H0N8N.

Family and domain databases

HAMAPiMF_01969. KynB. 1 hit.
InterProiIPR007325. KFase.
IPR017484. Kynurenine_formamidase_bac.
[Graphical view]
PfamiPF04199. Cyclase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2S2F5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALIDISRSV SPATAVWPGD QEVQWTWTAR RNEDESSVNL GSLRLSTHTG
60 70 80 90 100
THVDAPLHVK RQGQATDDLP LDSFVGPARV VDVNANAPSV RPEHIGQLDG
110 120 130 140 150
ASAERVLFKT SSGVSPDDEW PDAVVPIQPD TIHALADAGV SLVGTDAPSV
160 170 180 190 200
DPLDSTDLPA HHALLDTGIV NLEGLVLTNV PPGRYELIAL PLKIVGGDAA
210
PVRAVLRDAP DP
Length:212
Mass (Da):22,347
Last modified:January 24, 2006 - v1
Checksum:i8882F8F51EB21EF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000159 Genomic DNA. Translation: ABC46272.1.
RefSeqiWP_011404252.1. NC_007677.1.
YP_445626.1. NC_007677.1.

Genome annotation databases

EnsemblBacteriaiABC46272; ABC46272; SRU_1503.
GeneIDi3852572.
KEGGisru:SRU_1503.
PATRICi23425441. VBISalRub86502_1559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000159 Genomic DNA. Translation: ABC46272.1.
RefSeqiWP_011404252.1. NC_007677.1.
YP_445626.1. NC_007677.1.

3D structure databases

ProteinModelPortaliQ2S2F5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309807.SRU_1503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC46272; ABC46272; SRU_1503.
GeneIDi3852572.
KEGGisru:SRU_1503.
PATRICi23425441. VBISalRub86502_1559.

Phylogenomic databases

eggNOGiENOG4107XCH. Bacteria.
COG1878. LUCA.
HOGENOMiHOG000219455.
KOiK07130.
OMAiMDAHHRI.
OrthoDBiPOG091H0N8N.

Enzyme and pathway databases

UniPathwayiUPA00333; UER00454.
BioCyciSRUB309807:GJJD-1500-MONOMER.

Family and domain databases

HAMAPiMF_01969. KynB. 1 hit.
InterProiIPR007325. KFase.
IPR017484. Kynurenine_formamidase_bac.
[Graphical view]
PfamiPF04199. Cyclase. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKYNB_SALRD
AccessioniPrimary (citable) accession number: Q2S2F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: January 24, 2006
Last modified: September 7, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.