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Protein

Kynureninase 1

Gene

kyn-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway: L-kynurenine degradation

This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Kynureninase 1 (kyn-1), Kynureninase 2 (kyn-2)
This subpathway is part of the pathway L-kynurenine degradation, 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-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

Pathway: NAD(+) biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (nic-3)
  2. Kynureninase 1 (kyn-1), Kynureninase 2 (kyn-2)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (bna1)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei156 – 1561Pyridoxal phosphateUniRule annotation
Binding sitei267 – 2671Pyridoxal phosphateUniRule annotation
Binding sitei270 – 2701Pyridoxal phosphateUniRule annotation
Binding sitei292 – 2921Pyridoxal phosphateUniRule annotation
Binding sitei330 – 3301Pyridoxal phosphateUniRule annotation
Binding sitei358 – 3581Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
Kynureninase 1UniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5-1UniRule annotation
L-kynurenine hydrolase 1UniRule annotation
Gene namesi
Name:kyn-1
Synonyms:bna5-1
ORF Names:NCU09183
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 3, Linkage Group III

Organism-specific databases

EuPathDBiFungiDB:NCU09183.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Kynureninase 1PRO_0000356981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei293 – 2931N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi5141.EFNCRP00000009038.

Structurei

3D structure databases

ProteinModelPortaliQ7S332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 1864Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
InParanoidiQ7S332.
KOiK01556.
OMAiWDLSHAA.
OrthoDBiEOG7V1G0J.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7S332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDFTSKVKV LRDGQKPEFP SNANTLEYAQ SLDAQDELRH FRNEFIIPTR
60 70 80 90 100
ASLKKKALDG IIPGTQANGT TTSTDADTPC IYFVGNSLGA QPKAVRHYLE
110 120 130 140 150
AQLETWASIG VNGHFSSLSN SPLTPWQDMA ADCAAKSAAI VGAADPSEVV
160 170 180 190 200
IMNTLTVNLH FMMASFYRPT DKRHKIILEW RPFPSDWYAF QSQIEWHGLD
210 220 230 240 250
PEKSIVEMQP DENLYLSTEK ILATIDEHAE DAALLLLPGI QYYTGQLFDI
260 270 280 290 300
PRITKYAQER GIVVGWDLAH CAGNVELQLH DWNVDFAVWC TYKYLNGGPG
310 320 330 340 350
SMAGAFVHER HGKVDMSLGK PVFKPRLSGW YGADKSVRFN MDKEFQPTPG
360 370 380 390 400
AQGFQVSNPS AIDLTSLAAA LSVFNKTSMK DLRSKALVLT AYTEHLLDEI
410 420 430 440 450
VRRQPEGEEP AFKIITPRDP LQRGTQLSLL LRDGLMDKVA AALEENGVVC
460 470 480
DKRKPNVIRV APVPMYCRFE DVWKFMEIFE AAIRG
Length:485
Mass (Da):54,175
Last modified:December 15, 2003 - v1
Checksum:iCC38185722A45A37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002238 Genomic DNA. Translation: EAA29857.1.
RefSeqiXP_959093.1. XM_954000.1.

Genome annotation databases

EnsemblFungiiEFNCRT00000009056; EFNCRP00000009038; EFNCRG00000009041.
GeneIDi3875240.
KEGGincr:NCU09183.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002238 Genomic DNA. Translation: EAA29857.1.
RefSeqiXP_959093.1. XM_954000.1.

3D structure databases

ProteinModelPortaliQ7S332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.EFNCRP00000009038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000009056; EFNCRP00000009038; EFNCRG00000009041.
GeneIDi3875240.
KEGGincr:NCU09183.

Organism-specific databases

EuPathDBiFungiDB:NCU09183.

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
InParanoidiQ7S332.
KOiK01556.
OMAiWDLSHAA.
OrthoDBiEOG7V1G0J.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01970. Kynureninase.
InterProiIPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR14084. PTHR14084. 1 hit.
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF038800. KYNU. 1 hit.
SUPFAMiSSF53383. SSF53383. 2 hits.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiKYNU1_NEUCR
AccessioniPrimary (citable) accession number: Q7S332
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 15, 2003
Last modified: June 24, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

External Data

Dasty 3

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 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.