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KAT1_RAT
ID   KAT1_RAT                Reviewed;         423 AA.
AC   Q08415; Q9R096;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Kynurenine--oxoglutarate transaminase 1 {ECO:0000305|PubMed:7796908};
DE            Short=Kynurenine--oxoglutarate transaminase I;
DE            EC=2.6.1.7 {ECO:0000269|PubMed:2072101, ECO:0000269|PubMed:6783036, ECO:0000269|PubMed:7796908};
DE   AltName: Full=Cysteine-S-conjugate beta-lyase {ECO:0000305|PubMed:8502223};
DE            EC=4.4.1.13 {ECO:0000269|PubMed:8502223};
DE   AltName: Full=Glutamine transaminase K;
DE            Short=GTK;
DE   AltName: Full=Glutamine--phenylpyruvate transaminase {ECO:0000305|PubMed:8502223};
DE            EC=2.6.1.64 {ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223};
DE   AltName: Full=Kynurenine aminotransferase 1 {ECO:0000312|RGD:1306912};
DE   AltName: Full=Kynurenine aminotransferase I;
DE            Short=KATI;
GN   Name=Kyat1 {ECO:0000312|RGD:1306912}; Synonyms=Ccbl1, Kat;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 39-62; 228-259
RP   AND 388-401, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=8502223;
RA   Perry S.J., Schofield M.A., MacFarlane M., Lock E.A., King L.J.,
RA   Gibson G.G., Goldfarb P.S.;
RT   "Isolation and expression of a cDNA coding for rat kidney cytosolic
RT   cysteine conjugate beta-lyase.";
RL   Mol. Pharmacol. 43:660-665(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=7926014; DOI=10.1016/0014-5793(94)01003-x;
RA   Mosca M., Cozzi L., Breton J., Speciale C., Okuno E., Schwarcz R.,
RA   Benatti L.;
RT   "Molecular cloning of rat kynurenine aminotransferase: identity with
RT   glutamine transaminase K.";
RL   FEBS Lett. 353:21-24(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   PATHWAY, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND BIOPHYSICOCHEMICAL
RP   PROPERTIES (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   PubMed=7796908; DOI=10.1016/0014-5793(95)00546-l;
RA   Malherbe P., Alberati-Giani D., Koehler C., Cesura A.M.;
RT   "Identification of a mitochondrial form of kynurenine
RT   aminotransferase/glutamine transaminase K from rat brain.";
RL   FEBS Lett. 367:141-144(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=12850267; DOI=10.1016/s0167-4781(03)00071-x;
RA   Mosca M., Croci C., Mostardini M., Breton J., Malyszko J., Avanzi N.,
RA   Toma S., Benatti L., Gatti S.;
RT   "Tissue expression and translational control of rat kynurenine
RT   aminotransferase/glutamine transaminase K mRNAs.";
RL   Biochim. Biophys. Acta 1628:1-10(2003).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=6783036; DOI=10.1042/bj1890581;
RA   Okuno E., Minatogawa Y., Nakamura M., Kamoda N., Nakanishi J., Makino M.,
RA   Kido R.;
RT   "Crystallization and characterization of human liver kynurenine-glyoxylate
RT   aminotransferase. Identity with alanine-glyoxylate aminotransferase and
RT   serine-pyruvate aminotransferase.";
RL   Biochem. J. 189:581-590(1980).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=2072101; DOI=10.1111/j.1471-4159.1991.tb03783.x;
RA   Okuno E., Schmidt W., Parks D.A., Nakamura M., Schwarcz R.;
RT   "Measurement of rat brain kynurenine aminotransferase at physiological
RT   kynurenine concentrations.";
RL   J. Neurochem. 57:533-540(1991).
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC       metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in
CC       the tryptophan catabolic pathway which is also a broad spectrum
CC       antagonist of the three ionotropic excitatory amino acid receptors
CC       among others (PubMed:7796908, PubMed:6783036, PubMed:2072101).
CC       Metabolizes the cysteine conjugates of certain halogenated alkenes and
CC       alkanes to form reactive metabolites. Catalyzes the beta-elimination of
CC       S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the
CC       cleavage of the C-S or C-Se bond (PubMed:8502223).
CC       {ECO:0000269|PubMed:2072101, ECO:0000269|PubMed:6783036,
CC       ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC         glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC         ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000269|PubMed:2072101,
CC         ECO:0000269|PubMed:6783036, ECO:0000269|PubMed:7796908};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC         Evidence={ECO:0000305|PubMed:7796908};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpyruvate + L-glutamine = 2-oxoglutaramate + L-
CC         phenylalanine; Xref=Rhea:RHEA:17593, ChEBI:CHEBI:16769,
CC         ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:58359; EC=2.6.1.64;
CC         Evidence={ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC         Evidence={ECO:0000269|PubMed:8502223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC         Evidence={ECO:0000305|PubMed:8502223};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- ACTIVITY REGULATION: Inhibited by aminooxyacetate (in vitro).
CC       {ECO:0000269|PubMed:2072101}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=17 uM for L-kynurenine (with 2-oxoglutarate as cosubstrate)
CC         {ECO:0000269|PubMed:2072101};
CC         KM=910 uM for L-kynurenine (with pyruvate as cosubstrate)
CC         {ECO:0000269|PubMed:2072101};
CC         KM=150 uM for 2-oxoglutarate {ECO:0000269|PubMed:2072101};
CC         KM=160 uM for pyruvate {ECO:0000269|PubMed:2072101};
CC       pH dependence:
CC         Optimum pH is 9-9.5. {ECO:0000269|PubMed:6783036};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC       Kinetic parameters:
CC         KM=1630 uM for L-kynurenine (with 2-oxoglutarate as cosubstrate)
CC         {ECO:0000269|PubMed:7796908};
CC         KM=96.2 uM for L-kynurenine (with L-pyruvate as cosubstrate)
CC         {ECO:0000269|PubMed:7796908};
CC         Vmax=10.8 nmol/min/mg enzyme with L-kynurenine as substrate (with 2-
CC         oxoglutarate as cosubstrate) {ECO:0000269|PubMed:7796908};
CC         Vmax=0.39 nmol/min/mg enzyme with L-kynurenine as substrate (with L-
CC         pyruvate as cosubstrate) {ECO:0000269|PubMed:7796908};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC       from L-kynurenine: step 1/2. {ECO:0000305|PubMed:7796908}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6783036}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:7796908, ECO:0000269|PubMed:8502223}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix
CC       {ECO:0000269|PubMed:7796908}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=S-KAT/GTK {ECO:0000303|PubMed:7796908};
CC         IsoId=Q08415-2; Sequence=Displayed;
CC       Name=1; Synonyms=M-KAT/GTK {ECO:0000303|PubMed:7796908};
CC         IsoId=Q08415-1; Sequence=VSP_060909;
CC   -!- TISSUE SPECIFICITY: Detected in kidney. {ECO:0000269|PubMed:8502223}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; S61960; AAB26845.1; -; mRNA.
DR   EMBL; S74029; AAB32197.1; -; mRNA.
DR   EMBL; Z49696; CAA89696.1; -; mRNA.
DR   EMBL; AF100154; AAF06837.1; -; Genomic_DNA.
DR   EMBL; AF267749; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; S66270; S66270.
DR   RefSeq; NP_001013182.3; NM_001013164.3.
DR   AlphaFoldDB; Q08415; -.
DR   SMR; Q08415; -.
DR   STRING; 10116.ENSRNOP00000021865; -.
DR   iPTMnet; Q08415; -.
DR   PhosphoSitePlus; Q08415; -.
DR   jPOST; Q08415; -.
DR   PaxDb; Q08415; -.
DR   PRIDE; Q08415; -.
DR   GeneID; 311844; -.
DR   KEGG; rno:311844; -.
DR   UCSC; RGD:1306912; rat. [Q08415-2]
DR   CTD; 883; -.
DR   RGD; 1306912; Kyat1.
DR   eggNOG; KOG0257; Eukaryota.
DR   InParanoid; Q08415; -.
DR   OrthoDB; 683031at2759; -.
DR   PhylomeDB; Q08415; -.
DR   BRENDA; 2.6.1.7; 5301.
DR   Reactome; R-RNO-71240; Tryptophan catabolism.
DR   Reactome; R-RNO-8964208; Phenylalanine metabolism.
DR   Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR   SABIO-RK; Q08415; -.
DR   UniPathway; UPA00334; UER00726.
DR   PRO; PR:Q08415; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IDA:RGD.
DR   GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; IDA:RGD.
DR   GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006575; P:cellular modified amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
DR   GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0097052; P:L-kynurenine metabolic process; IDA:RGD.
DR   GO; GO:0006090; P:pyruvate metabolic process; IDA:RGD.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR034614; KAT_I.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43807:SF14; PTHR43807:SF14; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Aminotransferase; Cytoplasm;
KW   Direct protein sequencing; Lyase; Mitochondrion; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide.
FT   CHAIN           1..423
FT                   /note="Kynurenine--oxoglutarate transaminase 1"
FT                   /id="PRO_0000452095"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16773"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16773"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16773"
FT   MOD_RES         82
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BTY1"
FT   MOD_RES         247
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16773"
FT   VAR_SEQ         1
FT                   /note="M -> MFRSAAALSVHLMWPLWGRKAGASLTRCLHQSLTM (in isoform
FT                   1)"
FT                   /id="VSP_060909"
FT   CONFLICT        107
FT                   /note="R -> A (in Ref. 2; AAB32197 and 4; AAF06837)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="I -> V (in Ref. 2; AAB32197)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   423 AA;  47873 MW;  CEE7194633F96AA1 CRC64;
     MTKRLQARRL DGIDQNLWVE FGKLTKEYDV VNLGQGFPDF SPPDFATQAF QQATSGNFML
     NQYTRAFGYP PLTNVLASFF GKLLGQEMDP LTNVLVTVGA YGALFTRFQA LVDEGDEVII
     MEPAFDCYEP MTMMAGGCPV FVTLKPSPAP KGKLGASNDW QLDPAELASK FTPRTKILVL
     NTPNNPLGKV FSRMELELVA NLCQQHDVVC ISDEVYQWLV YDGHQHVSIA SLPGMWDRTL
     TIGSAGKSFS ATGWKVGWVM GPDNIMKHLR TVHQNSIFHC PTQAQAAVAQ CFEREQQHFG
     QPSSYFLQLP QAMELNRDHM IRSLQSVGLK LWISQGSYFL IADISDFKSK MPDLPGAEDE
     PYDRRFAKWM IKNMGLVGIP VSTFFSRPHQ KDFDHYIRFC FVKDKATLQA MDERLRKWKE
     LQP
 
 
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