AATM_RABIT
ID AATM_RABIT Reviewed; 430 AA.
AC P12345; G1SKL2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 134.
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;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke;
RG The Genome Sequencing Platform;
RA Di Palma F., Heiman D., Young S., Gnerre S., Johnson J., Lander E.S.,
RA Lindblad-Toh K.;
RT "Genome Sequence of Oryctolagus cuniculus (European rabbit).";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 30-59.
RC TISSUE=Liver;
RX PubMed=4030726; DOI=10.1093/oxfordjournals.jbchem.a135186;
RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.;
RT "Aspartate aminotransferase isozymes from rabbit liver. Purification and
RT properties.";
RL J. Biochem. 97:1337-1345(1985).
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; AAGW02052878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B27103; B27103.
DR RefSeq; XP_002711597.1; XM_002711551.3.
DR AlphaFoldDB; P12345; -.
DR SMR; P12345; -.
DR STRING; 9986.ENSOCUP00000003357; -.
DR GeneID; 100348732; -.
DR KEGG; ocu:100348732; -.
DR CTD; 2806; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR OMA; VGACTIV; -.
DR OrthoDB; 1104596at2759; -.
DR TreeFam; TF300641; -.
DR Proteomes; UP000001811; Unplaced.
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 GO; GO:0006457; P:protein folding; TAS:HGNC.
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 1: Evidence at protein level;
KW Acetylation; Aminotransferase; Cell membrane; Direct protein sequencing;
KW Lipid transport; Membrane; Methylation; Mitochondrion; Nitration;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide; Transport.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:4030726"
FT CHAIN 30..430
FT /note="Aspartate aminotransferase, mitochondrial"
FT /id="PRO_0000123886"
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 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 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; 12F54284974D27A5 CRC64;
MALLHSARVL SGVASAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA YKRDTNSKKM
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK GLDKEYLPIG GLAEFCRASA ELALGENSEV
VKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQSYR
YYDPKTCGFD FTGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVICKDADE
AKRVESQLKI LIRPMYSNPP IHGARIASTI LTSPDLRKQW LQEVKGMADR IIGMRTQLVS
NLKKEGSTHS WQHITDQIGM FCFTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY
LAHAIHQVTK
