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AATM_MACFA
ID   AATM_MACFA              Reviewed;         430 AA.
AC   Q4R559;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Aspartate aminotransferase, mitochondrial;
DE            Short=mAspAT;
DE            EC=2.6.1.1 {ECO:0000250|UniProtKB:P00507};
DE            EC=2.6.1.7 {ECO:0000250|UniProtKB:P00507};
DE   AltName: Full=Fatty acid-binding protein;
DE            Short=FABP-1;
DE   AltName: Full=Glutamate oxaloacetate transaminase 2;
DE   AltName: Full=Kynurenine aminotransferase 4;
DE   AltName: Full=Kynurenine aminotransferase IV;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase 4;
DE   AltName: Full=Kynurenine--oxoglutarate transaminase IV;
DE   AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE            Short=FABPpm;
DE   AltName: Full=Transaminase A;
DE   Flags: Precursor;
GN   Name=GOT2; ORFNames=QccE-17876;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC       metabolite L-kynurenine to form kynurenic acid (KA). As a member of the
CC       malate-aspartate shuttle, it has a key role in the intracellular NAD(H)
CC       redox balance. Is important for metabolite exchange between
CC       mitochondria and cytosol, and for amino acid metabolism. Facilitates
CC       cellular uptake of long-chain free fatty acids.
CC       {ECO:0000250|UniProtKB:P00505}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P00507};
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;
CC         Evidence={ECO:0000250|UniProtKB:P00507};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}. Cell membrane
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB169685; BAE01766.1; -; mRNA.
DR   RefSeq; NP_001270119.1; NM_001283190.1.
DR   AlphaFoldDB; Q4R559; -.
DR   SMR; Q4R559; -.
DR   STRING; 9541.XP_005592181.1; -.
DR   GeneID; 101867025; -.
DR   CTD; 2806; -.
DR   VEuPathDB; HostDB:ENSMFAG00000000866; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   OrthoDB; 1104596at2759; -.
DR   Proteomes; UP000233100; Chromosome 20.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; PTHR11879; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminotransferase; Cell membrane; Lipid transport; Membrane;
KW   Methylation; Mitochondrion; Nitration; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide; Transport.
FT   TRANSIT         1..29
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           30..430
FT                   /note="Aspartate aminotransferase, mitochondrial"
FT                   /id="PRO_0000278664"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         73
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         82
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         90
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         90
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         96
FT                   /note="3'-nitrotyrosine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         96
FT                   /note="Phosphotyrosine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         107
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         107
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         122
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         122
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         159
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         159
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         185
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         185
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         227
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         234
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         296
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         296
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         302
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         309
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         309
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P12344"
FT   MOD_RES         313
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         333
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         338
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         338
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         345
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         363
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         363
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         364
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         387
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         396
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         396
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
FT   MOD_RES         404
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P00505"
FT   MOD_RES         404
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P05202"
SQ   SEQUENCE   430 AA;  47409 MW;  CF155323BC4DB36A CRC64;
     MALLHSGRVL SGIAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
     NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENSEV
     LKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
     YYDPKTCGFD FTGAVEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
     FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTMVCKDADE
     AKRVESQLKI LIRPMYSNPP LNGARIAAAI LNTPDLRKQW LQEVKGMADR IIGMRTQLVS
     NLKKEGSTHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY
     LAHAIHQVTK
 
 
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