AAPAT_THEAQ
ID AAPAT_THEAQ Reviewed; 383 AA.
AC O33822; O31028;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Probable aspartate/prephenate aminotransferase {ECO:0000250|UniProtKB:Q56232};
DE Short=AspAT / PAT {ECO:0000250|UniProtKB:Q56232};
DE EC=2.6.1.1 {ECO:0000250|UniProtKB:Q56232};
DE EC=2.6.1.78 {ECO:0000250|UniProtKB:Q56232};
DE AltName: Full=Transaminase A;
GN Name=aspC;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=9367851; DOI=10.1006/bbrc.1997.7559;
RA O'Farrell P., Sannia G., Walker J.M., Doonan S.;
RT "Cloning and sequencing of aspartate aminotransferase from Thermus
RT aquaticus YT1.";
RL Biochem. Biophys. Res. Commun. 239:810-815(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RA Benner E., Ramaley R.F.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate. Can also transaminate
CC prephenate in the presence of aspartate.
CC {ECO:0000250|UniProtKB:Q56232}.
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:Q56232};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate;
CC Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78;
CC Evidence={ECO:0000250|UniProtKB:Q56232};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q56232};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q56232}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q56232}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X99521; CAA67877.1; -; Genomic_DNA.
DR EMBL; AF025665; AAB81842.1; -; Genomic_DNA.
DR PIR; JC5775; JC5775.
DR AlphaFoldDB; O33822; -.
DR SMR; O33822; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033853; F:aspartate-prephenate aminotransferase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT CHAIN 1..383
FT /note="Probable aspartate/prephenate aminotransferase"
FT /id="PRO_0000123855"
FT BINDING 39
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 125
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 175
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 361
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT SITE 12
FT /note="Important for prephenate aminotransferase activity"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT CONFLICT 18
FT /note="A -> V (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="E -> H (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..53
FT /note="AG -> RA (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> G (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="R -> G (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..187
FT /note="LR -> CE (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..220
FT /note="GT -> RH (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 230..231
FT /note="NG -> ER (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="K -> N (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="E -> D (in Ref. 2; AAB81842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 383 AA; 41717 MW; 5DD8E2769AA7835B CRC64;
MRGLSQRVKS MKPSATVAVN ARALELRRKG VDLVALTAGE PDFDTPEHVK EAGRRALAQG
KTKYAPPAGI PELREAVAEK FRRENGLEVT PEETIVTVGG KQALFNLFQA ILDPGDEVIV
LAPYWVSYPE MVRFAGGVPV EVPTLPEEGF VPDPERVRRA ITPRTKALVV NSPNNPTGVV
YPEEVLRALA EMALQHDFYL VSDEIYEHLI YEGAHFSPGT LAPEHTITVN GAAKAFAMTG
WRIGYACGPK AVIKAMADVS SQSTTSPDTI AQWATLEALT NREASMAFIA MAREAYRKRR
DLLLEGLSRI GLEAVRPSGA FYVLMDTSPF APNEVEAAER LLMAGVAVVP GTEFAAFGHV
RLSYATGEEN LKKALERFAQ ALQ
