AATC_CHICK
ID AATC_CHICK Reviewed; 412 AA.
AC P00504;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic {ECO:0000250|UniProtKB:P17174};
DE Short=cAspAT;
DE EC=2.6.1.1 {ECO:0000250|UniProtKB:P13221};
DE EC=2.6.1.3 {ECO:0000250|UniProtKB:P13221};
DE AltName: Full=Cysteine aminotransferase, cytoplasmic;
DE AltName: Full=Cysteine transaminase, cytoplasmic;
DE Short=cCAT;
DE AltName: Full=Glutamate oxaloacetate transaminase 1;
DE AltName: Full=Transaminase A;
GN Name=GOT1 {ECO:0000250|UniProtKB:P17174};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2503046; DOI=10.1016/0300-9084(89)90171-5;
RA Mattes U., Jaussi R., Ziak M., Juretic N., Lindenmann J.-M., Christen P.;
RT "Structure of cDNA of cytosolic aspartate aminotransferase of chicken and
RT its expression in E. coli.";
RL Biochimie 71:411-416(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-412, AND ACETYLATION AT ALA-2.
RC TISSUE=Heart;
RX PubMed=499525; DOI=10.1016/0014-5793(79)80537-2;
RA Shlyapnikov S.V., Myasnikov A.N., Severin E.S., Myagkova M.A.,
RA Torchinsky Y.M., Braunstein A.E.;
RT "Primary structure of cytoplasmic aspartate aminotransferase from chicken
RT heart and its homology with pig heart isoenzymes.";
RL FEBS Lett. 106:385-388(1979).
RN [3]
RP PROTEIN SEQUENCE OF 2-412.
RC TISSUE=Heart;
RA Shlyapnikov S.V., Myasnikov A.N., Severin E.S., Myagkova M.A.,
RA Demidkina T.V., Torchinsky Y.M., Braunstein A.E.;
RT "Primary structure of cytoplasmic aspartate aminotransferase from chicken
RT heart IV, Structure of cyanogen bromide peptides and the complete amino
RT acid sequence of the protein.";
RL Bioorg. Khim. 6:876-884(1980).
RN [4]
RP GENE STRUCTURE.
RC STRAIN=White leghorn;
RX PubMed=2401287; DOI=10.1111/j.1432-1033.1990.tb19204.x;
RA Juretic N., Mattes U., Ziak M., Christen P., Jaussi R.;
RT "Structure of the genes of two homologous intracellularly heterotopic
RT isoenzymes. Cytosolic and mitochondrial aspartate aminotransferase of
RT chicken.";
RL Eur. J. Biochem. 192:119-126(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE.
RX PubMed=7067826; DOI=10.1016/0014-5793(82)80407-9;
RA Harutyunyan E.G., Malashkevich V.N., Tersyan S.S., Kochkina V.M.,
RA Torchinsky Y.M., Braunstein A.E.;
RT "Three-dimensional structure at 3.2-A resolution of the complex of
RT cytosolic aspartate aminotransferase from chicken heart with 2-
RT oxoglutarate.";
RL FEBS Lett. 138:113-116(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=7360247; DOI=10.1038/284189a0;
RA Borisov V.V., Borisova S.N., Sosfenov N.I., Vainshtein B.K.;
RT "Electron density map of chicken heart cytosol aspartate transaminase at
RT 3.5-A resolution.";
RL Nature 284:189-190(1980).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE
RP AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-258, AND SUBUNIT.
RX PubMed=7897655; DOI=10.1006/jmbi.1994.0126;
RA Malashkevich V.N., Strokopytov B.V., Borisov V.V., Dauter Z., Wilson K.S.,
RA Torchinsky Y.M.;
RT "Crystal structure of the closed form of chicken cytosolic aspartate
RT aminotransferase at 1.9-A resolution.";
RL J. Mol. Biol. 247:111-124(1995).
CC -!- FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine.
CC Important regulator of levels of glutamate, the major excitatory
CC neurotransmitter of the vertebrate central nervous system. Acts as a
CC scavenger of glutamate in brain neuroprotection. The aspartate
CC aminotransferase activity is involved in hepatic glucose synthesis
CC during development and in adipocyte glyceroneogenesis. Using L-cysteine
CC as substrate, regulates levels of mercaptopyruvate, an important source
CC of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the
CC action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide
CC is an important synaptic modulator and neuroprotectant in the brain.
CC {ECO:0000250|UniProtKB:P13221}.
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:P13221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21825;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-cysteine = 2-oxo-3-sulfanylpropanoate + L-
CC glutamate; Xref=Rhea:RHEA:17441, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35235, ChEBI:CHEBI:57678; EC=2.6.1.3;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17442;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:70223, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:74359;
CC Evidence={ECO:0000250|UniProtKB:P17174};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70225;
CC Evidence={ECO:0000250|UniProtKB:P17174};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 3-sulfino-L-alanine = 3-sulfinopyruvate + L-
CC glutamate; Xref=Rhea:RHEA:70295, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:61085, ChEBI:CHEBI:140699;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70297;
CC Evidence={ECO:0000250|UniProtKB:P13221};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:7897655};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7067826,
CC ECO:0000269|PubMed:7897655}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X15636; CAA33646.1; -; mRNA.
DR PIR; S05583; XNCHDC.
DR RefSeq; NP_990652.1; NM_205321.1.
DR PDB; 1AAT; X-ray; 2.80 A; A/B=2-412.
DR PDB; 2CST; X-ray; 1.90 A; A/B=2-412.
DR PDBsum; 1AAT; -.
DR PDBsum; 2CST; -.
DR AlphaFoldDB; P00504; -.
DR SMR; P00504; -.
DR STRING; 9031.ENSGALP00000012086; -.
DR iPTMnet; P00504; -.
DR PaxDb; P00504; -.
DR GeneID; 396261; -.
DR KEGG; gga:396261; -.
DR CTD; 2805; -.
DR VEuPathDB; HostDB:geneid_396261; -.
DR eggNOG; KOG1412; Eukaryota.
DR InParanoid; P00504; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P00504; -.
DR Reactome; R-GGA-352875; Gluconeogenesis.
DR Reactome; R-GGA-372568; Amino acid metabolism.
DR EvolutionaryTrace; P00504; -.
DR PRO; PR:P00504; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR GO; GO:0047801; F:L-cysteine transaminase activity; ISS:UniProtKB.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006533; P:aspartate catabolic process; IEA:Ensembl.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IEA:Ensembl.
DR GO; GO:0019550; P:glutamate catabolic process to aspartate; IEA:Ensembl.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
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 3D-structure; Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Cytoplasm; Direct protein sequencing; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:499525, ECO:0000269|Ref.3"
FT CHAIN 2..412
FT /note="Aspartate aminotransferase, cytoplasmic"
FT /id="PRO_0000123884"
FT BINDING 38
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 140
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 194
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT BINDING 386
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:499525"
FT MOD_RES 258
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 63
FT /note="D -> N (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="Missing (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="W -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="D -> S (in Ref. 2; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..234
FT /note="SLD -> NLE (in Ref. 2; AA sequence and 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2CST"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:2CST"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2CST"
FT TURN 226..230
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2CST"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 277..292
FT /evidence="ECO:0007829|PDB:2CST"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 313..344
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:2CST"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:2CST"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2CST"
FT HELIX 397..410
FT /evidence="ECO:0007829|PDB:2CST"
SQ SEQUENCE 412 AA; 45935 MW; C55BEE72669078E1 CRC64;
MAASIFAAVP RAPPVAVFKL TADFREDGDS RKVNLGVGAY RTDEGQPWVL PVVRKVEQLI
AGDGSLNHEY LPILGLPEFR ANASRIALGD DSPAIAQKRV GSVQGLGGTG ALRIGAEFLR
RWYNGNNNTA TPVYVSSPTW ENHNSVFMDA GFKDIRTYRY WDAAKRGLDL QGLLDDMEKA
PEFSIFILHA CAHNPTGTDP TPDEWKQIAA VMKRRCLFPF FDSAYQGFAS GSLDKDAWAV
RYFVSEGFEL FCAQSFSKNF GLYNERVGNL SVVGKDEDNV QRVLSQMEKI VRTTWSNPPS
QGARIVATTL TSPQLFAEWK DNVKTMADRV LLMRSELRSR LESLGTPGTW NHITDQIGMF
SFTGLNPKQV EYMIKEKHIY LMASGRINMC GLTTKNLDYV AKSIHEAVTK IQ
