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Protein

Kynureninase

Gene

BNA5

Organism
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
Status
Unreviewed-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-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation
L-kynurenine + H2O = anthranilate + 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 (BNA5), Kynureninase (BNA5)
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 (BNA4)
  2. Kynureninase (BNA5), Kynureninase (BNA5)
  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 sitei156 – 1561Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei157 – 1571Pyridoxal phosphateUniRule annotation
Binding sitei270 – 2701Pyridoxal phosphateUniRule annotation
Binding sitei273 – 2731Pyridoxal phosphateUniRule annotation
Binding sitei295 – 2951Pyridoxal phosphateUniRule annotation
Binding sitei337 – 3371Pyridoxal phosphateUniRule annotation
Binding sitei365 – 3651Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Biological processi

Pyridine nucleotide biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
Biosynthesis of nicotinic acid protein 5UniRule annotation
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:BNA5UniRule annotation
ORF Names:SMAC_01897Imported
OrganismiSordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)Imported
Taxonomic identifieri771870 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria
ProteomesiUP000001881 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:SMAC_01897.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei296 – 2961N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi771870.XP_003348873.1.

Structurei

3D structure databases

ProteinModelPortaliF7VS63.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1884Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

InParanoidiF7VS63.
KOiK01556.
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. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.

Sequencei

Sequence statusi: Complete.

F7VS63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASSWPTNN DNHPTNSPAK WKNMSTAAVQ DARKQAEALD NEDPIAFIRD
60 70 80 90 100
EFNIPTKAQI ASSRLADSHP AALPASKDDA KSVYLCGNSL GVQPKRTVTR
110 120 130 140 150
LNQYLTTWAT QGVQGHFKPL EESPLPTWLD ADAKAAELIA PVVGADVSEV
160 170 180 190 200
AVMQTLTANI HLLMSAFYRP DINNRHKVIL ENKAFPSDHF VVETQIRHHS
210 220 230 240 250
LSTEKSMVLI DSSSKDNIIT TQEILSVISA HADTTALLLL PGIQYYTGQL
260 270 280 290 300
LDIPAITAFA HKHGIFVIWD LAHAVGNVPL YLHDWGVDAA AWCSYKYLNG
310 320 330 340 350
GPGCIGGLFV HTNNSIVTKE ITDEKPEEGY SNRLAGWWGN DKKTRFVMAN
360 370 380 390 400
KFHPVAGAAG FQLSNPSILD ITSLSASLEI FQEAGGMEAL RSKSLKLTNF
410 420 430 440 450
LEATLGGMKE EDRAHFRIIT PSKPEERGAQ LSLMLSDGLL DTVMKELEAR
460 470 480 490
GVIVDERRPN VIRVAPAPLY NTFSDCVQFV EAFSAALEAA TKRAL
Length:495
Mass (Da):54,196
Last modified:September 21, 2011 - v1
Checksum:i76235340CF95BE8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CABT02000005 Genomic DNA. Translation: CCC08349.1.
RefSeqiXP_003348873.1. XM_003348825.1.

Genome annotation databases

GeneIDi10806334.
KEGGismp:SMAC_01897.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CABT02000005 Genomic DNA. Translation: CCC08349.1.
RefSeqiXP_003348873.1. XM_003348825.1.

3D structure databases

ProteinModelPortaliF7VS63.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi771870.XP_003348873.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10806334.
KEGGismp:SMAC_01897.

Organism-specific databases

EuPathDBiFungiDB:SMAC_01897.

Phylogenomic databases

InParanoidiF7VS63.
KOiK01556.
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. 1 hit.
TIGRFAMsiTIGR01814. kynureninase. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis."
    Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K., Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S., Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.
    PLoS Genet. 6:E1000891-E1000891(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hellImported.
    Tissue: MyceliumImported.

Entry informationi

Entry nameiF7VS63_SORMK
AccessioniPrimary (citable) accession number: F7VS63
Entry historyi
Integrated into UniProtKB/TrEMBL: September 21, 2011
Last sequence update: September 21, 2011
Last modified: June 24, 2015
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.