ID   AAPAT_RICCN             Reviewed;         401 AA.
AC   Q92JE7;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable aspartate/prephenate aminotransferase {ECO:0000250|UniProtKB:Q02635};
DE            Short=AspAT / PAT {ECO:0000250|UniProtKB:Q02635};
DE            EC=2.6.1.1 {ECO:0000250|UniProtKB:Q02635};
DE            EC=2.6.1.79 {ECO:0000250|UniProtKB:Q02635};
DE   AltName: Full=Transaminase A;
GN   Name=aatA; Synonyms=aspC; OrderedLocusNames=RC0120;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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 glutamate.
CC       {ECO:0000250|UniProtKB:Q02635}.
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:Q02635};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate;
CC         Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79;
CC         Evidence={ECO:0000250|UniProtKB:Q02635};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q02635};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q02635}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q02635}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE006914; AAL02658.1; -; Genomic_DNA.
DR   PIR; H97714; H97714.
DR   RefSeq; WP_010976800.1; NC_003103.1.
DR   AlphaFoldDB; Q92JE7; -.
DR   SMR; Q92JE7; -.
DR   EnsemblBacteria; AAL02658; AAL02658; RC0120.
DR   KEGG; rco:RC0120; -.
DR   PATRIC; fig|272944.4.peg.142; -.
DR   HOGENOM; CLU_017584_4_3_5; -.
DR   OMA; SVAMTGW; -.
DR   Proteomes; UP000000816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033854; F:glutamate-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:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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..401
FT                   /note="Probable aspartate/prephenate aminotransferase"
FT                   /id="PRO_0000123850"
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         375
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         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q56232"
SQ   SEQUENCE   401 AA;  44576 MW;  580494ECD865CF36 CRC64;
     MSIISTRLSS IKPSPTLAVV KKTLELKKAG VDIITLGAGE PDFDTPDNIK EGAIKAIKDG
     FTKYTNVEGM PLLKQAIKDK FKRENNIDYE LDEIIVSTGG KQVIYNLFMA SLDQGDEVII
     PAPYWVSYPD MVALSTGTPV FVNCGIENNF KLSAEALERS ITDKTKWLII NSPSNPTGAS
     YNFEELENIA KVLRKYSHVN VMSDDIYEHI TFDDFKFYTL AQIAPDLKKR IFTVNGVSKA
     YSMTGWRIGY GAGSKTLIKA MTIIQSQSTS NPCSISQMAA IEALNGPQDY IKPNALNCQK
     KRDLALSILK RVKYFECYKP EGAFYLFVKC DKIFGHKTKS GTIIANSNDF AEYLLEEAKV
     AVVPGIAFGL EGYFRISYAT SMEELEKACI RIEKTIDVIP A