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Q736W3

- KYNU_BACC1

UniProt

Q736W3 - KYNU_BACC1

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Protein

Kynureninase

Gene

kynU

Organism
Bacillus cereus (strain ATCC 10987)
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

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:BCE_2787
OrganismiBacillus cereus (strain ATCC 10987)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527: 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_0000356988Add
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

STRINGi222523.BCE_2787.

Structurei

3D structure databases

ProteinModelPortaliQ736W3.
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.
OMAiHVAYRSA.
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.

Q736W3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYTEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA
60 70 80 90 100
EKSLLTLLDS WKEYGIDGWT EGEHPWFFLS EKLGELTAPL IGALPEETIV
110 120 130 140 150
TGSTTTNIHQ VIATFYEPKG IRTKILADEL TFPSDIYALQ SQIRLKGLDP
160 170 180 190 200
DEHLVRVKSR DGRTLSEDDI IHAMTDDIAL ILLPSVLYRS GQVLDMKRLT
210 220 230 240 250
AEAHKRGIHI GFDLCHSIGS IPHHFKEWDV DFAIWCNYKY LNAGPGGVAG
260 270 280 290 300
LYVNKKHCNR LPGLSGWFSS RKDKQFDMEH TLTAADHAGA YQIGTPHVLS
310 320 330 340 350
TAPLIGSLEI FKEAGIERLR EKSLHITSYM LNLIAHELSD FEFTIGNPLE
360 370 380 390 400
DEKRGGHIYL EHAEAARICK ALKADGVIPD FRAPNGVRLA PVALYNTYEE
410 420
VWKSVQILKK IMKDEEYKQF ENKREVVA
Length:428
Mass (Da):48,542
Last modified:July 5, 2004 - v1
Checksum:iB3910FB7D179773C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41699.1.
RefSeqiNP_979091.1. NC_003909.8.
WP_000287845.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS41699; AAS41699; BCE_2787.
GeneIDi2749806.
KEGGibca:BCE_2787.
PATRICi18854318. VBIBacCer118379_2659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41699.1 .
RefSeqi NP_979091.1. NC_003909.8.
WP_000287845.1. NC_003909.8.

3D structure databases

ProteinModelPortali Q736W3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 222523.BCE_2787.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS41699 ; AAS41699 ; BCE_2787 .
GeneIDi 2749806.
KEGGi bca:BCE_2787.
PATRICi 18854318. VBIBacCer118379_2659.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00329 .
UPA00334 ; UER00455 .

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. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987.

Entry informationi

Entry nameiKYNU_BACC1
AccessioniPrimary (citable) accession number: Q736W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 71 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