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Database: UniProt/TrEMBL
Entry: Q0APM4_MARMM
LinkDB: Q0APM4_MARMM
Original site: Q0APM4_MARMM 
ID   Q0APM4_MARMM            Unreviewed;       409 AA.
AC   Q0APM4;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   07-JUN-2017, entry version 75.
DE   RecName: Full=Kynureninase {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE            EC=3.7.1.3 {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800};
DE   AltName: Full=L-kynurenine hydrolase {ECO:0000256|HAMAP-Rule:MF_01970};
GN   Name=kynU {ECO:0000256|HAMAP-Rule:MF_01970};
GN   OrderedLocusNames=Mmar10_1471 {ECO:0000313|EMBL:ABI65763.1};
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI65763.1, ECO:0000313|Proteomes:UP000001964};
RN   [1] {ECO:0000313|EMBL:ABI65763.1, ECO:0000313|Proteomes:UP000001964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10 {ECO:0000313|EMBL:ABI65763.1,
RC   ECO:0000313|Proteomes:UP000001964};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-
CC       hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-
CC       hydroxyanthranilic acid (3-OHAA), respectively.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3-
CC       hydroxyanthranilate + L-alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L-
CC       alanine. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01970,
CC         ECO:0000256|PIRNR:PIRNR038800};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L-
CC       alanine and anthranilate from L-kynurenine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate
CC       from L-kynurenine: step 2/3. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01970,
CC       ECO:0000256|PIRNR:PIRNR038800}.
CC   -!- SIMILARITY: Belongs to the kynureninase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01970, ECO:0000256|PIRNR:PIRNR038800}.
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DR   EMBL; CP000449; ABI65763.1; -; Genomic_DNA.
DR   RefSeq; WP_011643410.1; NC_008347.1.
DR   ProteinModelPortal; Q0APM4; -.
DR   STRING; 394221.Mmar10_1471; -.
DR   EnsemblBacteria; ABI65763; ABI65763; Mmar10_1471.
DR   KEGG; mmr:Mmar10_1471; -.
DR   eggNOG; ENOG4105CKY; Bacteria.
DR   eggNOG; COG3844; LUCA.
DR   HOGENOM; HOG000242437; -.
DR   KO; K01556; -.
DR   OMA; VCSLHAS; -.
DR   OrthoDB; POG091H0D63; -.
DR   UniPathway; UPA00253; UER00329.
DR   UniPathway; UPA00334; UER00455.
DR   Proteomes; UP000001964; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030429; F:kynureninase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043420; P:anthranilate metabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006569; P:tryptophan catabolic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01970; Kynureninase; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010111; Kynureninase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR14084; PTHR14084; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF038800; KYNU; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01814; kynureninase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001964};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800, ECO:0000313|EMBL:ABI65763.1};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01970,
KW   ECO:0000256|PIRNR:PIRNR038800};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001964}.
FT   DOMAIN       78    357       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
FT   REGION      125    128       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      97     97       Pyridoxal phosphate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
FT   BINDING      98     98       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     167    167       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     196    196       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     199    199       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     221    221       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     251    251       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   BINDING     277    277       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01970}.
FT   MOD_RES     222    222       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01970}.
SQ   SEQUENCE   409 AA;  44383 MW;  6F0B57FC692FDC9C CRC64;
     MTTLDDARRL DTADPLAGFR ERFALPDSVI YLDGNSLGAL PKATSGRVEA VVQSEWGEDL
     IRAWNTRDWI SAPKRLGDKI ARLIGAAPGE VIAGESTSVN IFKALCACLQ LTPERSVILS
     ETGNFPTDAY MMEGLAALSG GRIRQVLVER DAIDAALTDD VAALLLTHTH YKSGQLHDMK
     AVTARAQALG IPVIWDLSHS AGAMPVALND CEADFAVGCG YKYLNGGPGA PAFLFVAKRH
     QDRVFPVLSG WLGHARPFDF DDRYEPAAGI DRFQCGTPAI LGMAALECGV DILLDADMQE
     IRIKSQALGD LFIEQVEDRL DGFELRSPRA AGERGSQVSF AHEHGYAIMQ ALIERGVIGD
     FRAPDILRFG FTPLYAGYAD VWTAVDILAD VMQSGVWQDA RFNIRSAVT
//
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