AAT_BACY2
ID AAT_BACY2 Reviewed; 392 AA.
AC P23034;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
OS Bacillus sp. (strain YM-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=72580;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1990006; DOI=10.1016/s0021-9258(18)52282-1;
RA Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Hirotsu K.,
RA Okamoto A., Higuchi T., Soda K.;
RT "Thermostable aspartate aminotransferase from a thermophilic Bacillus
RT species. Gene cloning, sequence determination, and preliminary X-ray
RT characterization.";
RL J. Biol. Chem. 266:2567-2572(1991).
RN [2]
RP PROTEIN SEQUENCE OF 1-24 AND 387-392.
RX PubMed=2155199; DOI=10.1128/jb.172.3.1345-1351.1990;
RA Sung M.H., Tanizawa K., Tanaka H., Kuramitsu S., Kagamiyama H., Soda K.;
RT "Purification and characterization of thermostable aspartate
RT aminotransferase from a thermophilic Bacillus species.";
RL J. Bacteriol. 172:1345-1351(1990).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Thermostable.;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M59430; AAA22250.1; -; Genomic_DNA.
DR AlphaFoldDB; P23034; -.
DR SMR; P23034; -.
DR SABIO-RK; P23034; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Direct protein sequencing;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..392
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123834"
FT BINDING 40
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 388
FT /note="D -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 42662 MW; 0384C74F655F85F4 CRC64;
MKELLANRVK TLTPSTTLAI TAKAKEMKAQ GIDVIGLGAG EPDFNTPQNI MDAAIDSMQQ
GYTKYTPSGG LPALKQAIIE KFKRDNQLEY KPNEIIVGVG AKHVLYTLFQ VILNEGDEVI
IPIPYWVSYP EQVKLAGGVP VYIEATSEQN YKITAEQLKN AITDKTKAVI INSPSNPTGM
VYTREELEDI AKIALENNIL IVSDEIYEKL LYNGAEHFSI AQISEEVKAQ TIVINGVSKS
HSMTGWRIGY AAGNADIINA MTDLASHSTS NPTTASQYAA IEAYNGPQDS VEEMRKAFES
RLETIYPKLS AIPGFKVVKP QGAFYLLPDV SEAAQKTGFA SVDEFASALL TEANVAVIPG
SGFGAPSTIR ISYATSLNLI EEAIERIDRF VK
