ID AAPAT_RICTY Reviewed; 399 AA.
AC Q68XV9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 09-APR-2025, entry version 99.
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; OrderedLocusNames=RT0046;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate;
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=L-arogenate + 2-oxoglutarate = prephenate + L-glutamate;
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; AE017197; AAU03533.1; -; Genomic_DNA.
DR RefSeq; WP_011190520.1; NC_006142.1.
DR AlphaFoldDB; Q68XV9; -.
DR SMR; Q68XV9; -.
DR KEGG; rty:RT0046; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OrthoDB; 9804407at2; -.
DR Proteomes; UP000000604; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR FunFam; 3.40.640.10:FF:000033; Aspartate aminotransferase; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II_large.
DR InterPro; IPR050596; AspAT/PAT-like.
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 PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT CHAIN 1..399
FT /note="Probable aspartate/prephenate aminotransferase"
FT /id="PRO_0000273126"
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 399 AA; 44337 MW; B070EBE4775C43B8 CRC64;
MSIISTRLNS IKPSPTLAVV KKTLELKKAG VNIIALGAGE PDFDTPDNIK EVAITSIKDG
FTKYTNVDGI PLLKQAIKNK FKRENNIDYE LDEIIVSTGG KQVIYNLFMA SLDKGDEVII
PVPYWVSYPD MVALSTGTPI FVNCGIENNF KLTVEALERS ITDKTKWLII NSPSNPTGAG
YNCKELENIA KTLRKYPNVN IMSDDIYEHI TFDDFKFYTL AQIAPDLKER IFTVNGVSKA
YSMTGWRIGY GAGSKALIKA MTVIQSQSTS NPCSISQMAA IEALNGTQDY IKPNALNFQK
KRDLALSILE KVIYFECYKP EGAFYLFVKC DKIFGTKTKS GKIIANSNHF SEYLLEEAKV
AVVPGVAFGL DGYFRISYAT SMQELKEACI RIKQACNTL
//
