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Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase)

 A0A1Q5ZWQ7_9SPHI        Unreviewed;       428 AA.
A0A1Q5ZWQ7;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
27-SEP-2017, entry version 5.
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=RG47T_1643 {ECO:0000313|EMBL:OKS86192.1};
Mucilaginibacter polytrichastri.
Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
Sphingobacteriaceae; Mucilaginibacter.
NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS86192.1, ECO:0000313|Proteomes:UP000186720};
[1] {ECO:0000313|EMBL:OKS86192.1, ECO:0000313|Proteomes:UP000186720}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RG4-7 {ECO:0000313|EMBL:OKS86192.1,
ECO:0000313|Proteomes:UP000186720};
Li Y.;
"Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
isolated from the moss sample.";
Submitted (NOV-2016) 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:OKS86192.1}.
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EMBL; MPPL01000001; OKS86192.1; -; Genomic_DNA.
RefSeq; WP_074488917.1; NZ_MPPL01000001.1.
UniPathway; UPA00253; UER00329.
UniPathway; UPA00334; UER00455.
Proteomes; UP000186720; 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:UP000186720};
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};
Reference proteome {ECO:0000313|Proteomes:UP000186720}.
DOMAIN 88 352 Aminotran_5. {ECO:0000259|Pfam:PF00266}.
REGION 133 136 Pyridoxal phosphate binding.
{ECO:0000256|HAMAP-Rule:MF_01970}.
BINDING 105 105 Pyridoxal phosphate; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_01970}.
BINDING 106 106 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 218 218 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 221 221 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 243 243 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 274 274 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
BINDING 302 302 Pyridoxal phosphate. {ECO:0000256|HAMAP-
Rule:MF_01970}.
MOD_RES 244 244 N6-(pyridoxal phosphate)lysine.
{ECO:0000256|HAMAP-Rule:MF_01970}.
SEQUENCE 428 AA; 47862 MW; 123BFD7B1EE070FD CRC64;
MNFENSLSFA QSLDASDQFR NLREEFYIPQ HKGNDAIYLC GNSLGLQPKS TETIIMSQLA
AWRNLGVEGW FEGDEPWLQY HKKLIGPLAK IVGAQAHEIA VMNSLTVNLH LLMVSFYKPT
SKKYKILMEA GAFPSDQYAV ESQVKFHGFE LADAIIEIAP REGEYTLRIE DIIVQINANA
DEVALVLFAG INYYTGQIFD MKAITAAGHQ AGAYVGFDLA HAAGNVPLSL HEWGADFACW
CSYKYMNSGP GGISGIFVHE KHHHDTSLDR FAGWWGYKLK DRFKMTPGFQ PEAGAEGWQV
STSPILLMAS LNASLQIFEK AGSVTALNKK SILLTAYLEY LIKQVNKQLN YEHFKIITPA
NQQERGSQLS LICKSDGKAI FDYLVSNGVI GDWREPDVIR LSPVPLYNSF EDVYQAAKYL
LEAVKHVQ


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