ID   AAPAT_AQUAE             Reviewed;         394 AA.
AC   O67781;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
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; OrderedLocusNames=aq_1969;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07746.1; -; Genomic_DNA.
DR   PIR; A70469; A70469.
DR   RefSeq; NP_214350.1; NC_000918.1.
DR   RefSeq; WP_010881286.1; NC_000918.1.
DR   AlphaFoldDB; O67781; -.
DR   SMR; O67781; -.
DR   STRING; 224324.aq_1969; -.
DR   EnsemblBacteria; AAC07746; AAC07746; aq_1969.
DR   KEGG; aae:aq_1969; -.
DR   PATRIC; fig|224324.8.peg.1521; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_3_0; -.
DR   InParanoid; O67781; -.
DR   OMA; SVAMTGW; -.
DR   OrthoDB; 554560at2; -.
DR   Proteomes; UP000000798; Chromosome.
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; 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.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..394
FT                   /note="Probable aspartate/prephenate aminotransferase"
FT                   /id="PRO_0000123833"
FT   BINDING         40
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P00509"
FT   BINDING         126
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   BINDING         176
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   BINDING         370
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   SITE            13
FT                   /note="Important for prephenate aminotransferase activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
FT   MOD_RES         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
SQ   SEQUENCE   394 AA;  43777 MW;  E570B4FD080C56E1 CRC64;
     MRKGLASRVS HLKPSPTLTI TAKAKELRAK GVDVIGFGAG EPDFDTPDFI KEACIRALRE
     GKTKYAPSAG IPELREAIAE KLLKENKVEY KPSEIVVSAG AKMVLFLIFM AILDEGDEVL
     LPSPYWVTYP EQIRFFGGVP VEVPLKKEKG FQLSLEDVKE KVTERTKAIV INSPNNPTGA
     VYEEEELKKI AEFCVERGIF IISDECYEYF VYGDAKFVSP ASFSDEVKNI TFTVNAFSKS
     YSMTGWRIGY VACPEEYAKV IASLNSQSVS NVTTFAQYGA LEALKNPKSK DFVNEMRNAF
     ERRRDTAVEE LSKIPGMDVV KPEGAFYIFP DFSAYAEKLG GDVKLSEFLL EKAKVAVVPG
     SAFGAPGFLR LSYALSEERL VEGIRRIKKA LEEI