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Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)

 J8B053_BACCE            Unreviewed;       428 AA.
J8B053;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
27-SEP-2017, entry version 31.
RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
ORFNames=IEE_02589 {ECO:0000313|EMBL:EJQ44399.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ44399.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ44399.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ44399.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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.
{ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800};
-!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
alanine and anthranilate from L-kynurenine: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
-!- SIMILARITY: Belongs to the kynureninase family.
{ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01970}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJQ44399.1}.
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EMBL; AHDJ01000027; EJQ44399.1; -; Genomic_DNA.
RefSeq; WP_002200277.1; NZ_JH791996.1.
EnsemblBacteria; EJQ44399; EJQ44399; IEE_02589.
PATRIC; fig|1053189.3.peg.2633; -.
UniPathway; UPA00253; UER00329.
UniPathway; UPA00334; UER00455.
Proteomes; UP000006600; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-UniRule.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-UniRule.
GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-UniRule.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
HAMAP; MF_01970; Kynureninase; 1.
InterPro; IPR000192; Aminotrans_V_dom.
InterPro; IPR010111; Kynureninase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR14084; PTHR14084; 1.
Pfam; PF00266; Aminotran_5; 1.
PIRSF; PIRSF038800; KYNU; 1.
SUPFAM; SSF53383; SSF53383; 1.
TIGRFAMs; TIGR01814; kynureninase; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000006600};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800};
Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970,
ECO:0000256|PIRNR:PIRNR038800}.
DOMAIN 85 372 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 132 135 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01970}.
BINDING 104 104 Pyridoxal phosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01970}.
BINDING 105 105 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 213 213 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 216 216 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 238 238 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 267 267 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 295 295 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
MOD_RES 239 239 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_01970}.
SEQUENCE 428 AA; 48594 MW; 9201CD403CD8339F CRC64;
MYKEPFQPTY EYALECDKHD ELKDFQTEFY KKEGTIYLDG NSLGLLSKRA EKSLLTLLDS
WKEFGIDGWT EGEHPWFFLS EKLGELTAPL IGALPEETIV TGSTTANIHQ VIATFYEPKG
IRTKILADEL TFPSDIYALQ SQIRLKGLDP DEHLVRVKSR DGRTLSEDDI IQAMTDDIAL
ILLPSVLYRS GQILDMKRLT AEAHKRGIHI GFDLCHSIGS IPHHFNEWDV DFAVWCNYKY
LNAGPGGVAG LYVNKKHLDR LPGLSGWFSS RKDKQFDMEH SLTAADHAGA YQIGTPHVLS
IAPLIGSLEI FKDARIERLR EKSLHITRYM LDLIQLELND MGFTIGNPLE DEKRGGHIYL
EHAEAARICK ALKANGVIPD FRAPNGVRLA PVALYNTYEE VWNSVQTLKK IMKNEEYKNF
ENKREVVA


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