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A7GPY3

- KYNU_BACCN

UniProt

A7GPY3 - KYNU_BACCN

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Protein

Kynureninase

Gene

kynU

Organism
Bacillus cereus subsp. cytotoxis (strain NVH 391-98)
Status
Reviewed - 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei104 – 1041Pyridoxal phosphate; via amide nitrogenUniRule annotation
Binding sitei105 – 1051Pyridoxal phosphateUniRule annotation
Binding sitei213 – 2131Pyridoxal phosphateUniRule annotation
Binding sitei216 – 2161Pyridoxal phosphateUniRule annotation
Binding sitei238 – 2381Pyridoxal phosphateUniRule annotation
Binding sitei267 – 2671Pyridoxal phosphateUniRule annotation
Binding sitei295 – 2951Pyridoxal phosphateUniRule annotation

GO - Molecular functioni

  1. kynureninase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. L-kynurenine catabolic process Source: UniProtKB-UniPathway
  4. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  5. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBCYT315749:GH2A-2016-MONOMER.
UniPathwayiUPA00253; UER00329.
UPA00334; UER00455.

Names & Taxonomyi

Protein namesi
Recommended name:
KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
Alternative name(s):
L-kynurenine hydrolaseUniRule annotation
Gene namesi
Name:kynUUniRule annotation
Ordered Locus Names:Bcer98_1903
OrganismiBacillus cereus subsp. cytotoxis (strain NVH 391-98)
Taxonomic identifieri315749 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002300: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428KynureninasePRO_0000356989Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi315749.Bcer98_1903.

Structurei

3D structure databases

ProteinModelPortaliA7GPY3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 1354Pyridoxal phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the kynureninase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3844.
HOGENOMiHOG000242438.
KOiK01556.
OMAiSYREEFY.
OrthoDBiEOG6N67XP.

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.

A7GPY3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDQNPFEASY EYAIQSDKQD ELAAFQNEFY KKADTIYLDG NSLGLLSKRA
60 70 80 90 100
EKSLLTMLNS WKEHGIDGWT EGEYPWFFLS EQLSEHIAPL IGALSEEIIV
110 120 130 140 150
TGSTTTNIHQ VIATFYEPKG IRTKILADEL TFPSDIYALQ SQIRLKGLDP
160 170 180 190 200
NEHLVRVKSR DGRTLDEEDI IAAMTDDIAL ILLPAVLYRS GQILDMKRLT
210 220 230 240 250
AEAHKRGIHI GFDLCHSIGA IPHQFQEWGV DFAVWCNYKY LNAGPGSVGG
260 270 280 290 300
LYVNKKHFAR LPGLSGWFSS RKDKQFDMEH TLTAAEHAGA YQIGTPHIFS
310 320 330 340 350
IAPLIGSLEI FKEAGIDRLR QKSLHITRYM LHLIDYELTD KGFTIGNPLE
360 370 380 390 400
DEKRGGHIYL EHPEAARICK ALKANGVIPD FRAPNGIRLA PVALYNTYEE
410 420
VWKSVRILKK IMTNEEYKQF ENKRGVVA
Length:428
Mass (Da):48,442
Last modified:September 11, 2007 - v1
Checksum:i84577A7CA0A046FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS22191.1.
RefSeqiYP_001375186.1. NC_009674.1.

Genome annotation databases

EnsemblBacteriaiABS22191; ABS22191; Bcer98_1903.
GeneIDi5345277.
KEGGibcy:Bcer98_1903.
PATRICi18932334. VBIBacCyt128034_2011.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS22191.1 .
RefSeqi YP_001375186.1. NC_009674.1.

3D structure databases

ProteinModelPortali A7GPY3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 315749.Bcer98_1903.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS22191 ; ABS22191 ; Bcer98_1903 .
GeneIDi 5345277.
KEGGi bcy:Bcer98_1903.
PATRICi 18932334. VBIBacCyt128034_2011.

Phylogenomic databases

eggNOGi COG3844.
HOGENOMi HOG000242438.
KOi K01556.
OMAi SYREEFY.
OrthoDBi EOG6N67XP.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .
BioCyci BCYT315749:GH2A-2016-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_01970. Kynureninase.
InterProi IPR000192. Aminotrans_V_dom.
IPR010111. Kynureninase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR14084. PTHR14084. 1 hit.
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF038800. KYNU. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01814. kynureninase. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NVH 391-98.

Entry informationi

Entry nameiKYNU_BACCN
AccessioniPrimary (citable) accession number: A7GPY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: September 11, 2007
Last modified: November 26, 2014
This is version 53 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3