AATC2_BOVIN
ID AATC2_BOVIN Reviewed; 407 AA.
AC Q2T9S8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative aspartate aminotransferase, cytoplasmic 2;
DE EC=2.6.1.1;
DE AltName: Full=Glutamate oxaloacetate transaminase 1-like protein 1;
DE AltName: Full=Transaminase A-like protein 1;
GN Name=GOT1L1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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}.
CC -!- CAUTION: The residues that bind the substrate in other aspartate
CC aminotransferases are not conserved. {ECO:0000305}.
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DR EMBL; BC111285; AAI11286.1; -; mRNA.
DR RefSeq; NP_001033147.1; NM_001038058.1.
DR AlphaFoldDB; Q2T9S8; -.
DR SMR; Q2T9S8; -.
DR STRING; 9913.ENSBTAP00000021864; -.
DR PaxDb; Q2T9S8; -.
DR PRIDE; Q2T9S8; -.
DR Ensembl; ENSBTAT00000021864; ENSBTAP00000021864; ENSBTAG00000016446.
DR GeneID; 507913; -.
DR KEGG; bta:507913; -.
DR CTD; 137362; -.
DR VEuPathDB; HostDB:ENSBTAG00000016446; -.
DR VGNC; VGNC:29502; GOT1L1.
DR eggNOG; KOG1412; Eukaryota.
DR GeneTree; ENSGT00950000183082; -.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; Q2T9S8; -.
DR OMA; LAYKVCM; -.
DR OrthoDB; 1104596at2759; -.
DR TreeFam; TF314089; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000016446; Expressed in spermatid and 58 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006532; P:aspartate biosynthetic process; IBA:GO_Central.
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; 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.
PE 2: Evidence at transcript level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..407
FT /note="Putative aspartate aminotransferase, cytoplasmic 2"
FT /id="PRO_0000332998"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 45918 MW; 0509D33422969661 CRC64;
MPTLSVFTDV PMAQKLEGSL LKTYKQDDNP NKMFLAYKVC MTSKGRPWVS SVVRKTRMQI
AQDPSLNYEY TPVMGMKSFV QASLNLLFGK NSQVIVENRA GGVQTVGDSG AFQLGAQFLK
SWCQSSQIVY IVSSQKEPHG LIFQDMGFTV YEHTFWDSAH LCLDPNMLLD VVKHAPHGCV
FVIGSMGNCQ LTPSQWTQLM TLMKSKEIFP FFDIPYQGLS TGDLEEDARF LHYFVSQGFE
FFCSQSLSKN FGIYDEGVGT LVVVTLDNQL LLRVLSQLMN FARALWLNPP TTGARIITSV
LCNPAMQGEW RQSLEGVVEN VMMTKEKVKE KLRLLGTPGS WDHITEQKGS HSYLGLNSQQ
VEYLISEKHI YIPKNGRINF TCINSYNIDY ITSSINEAVC FTKDSER