AAPAT_RICPR
ID AAPAT_RICPR Reviewed; 399 AA.
AC Q9ZE56;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
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=RP091;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(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 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA14561.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ235270; CAA14561.1; ALT_INIT; Genomic_DNA.
DR PIR; B71718; B71718.
DR RefSeq; NP_220484.1; NC_000963.1.
DR RefSeq; WP_014411730.1; NC_000963.1.
DR AlphaFoldDB; Q9ZE56; -.
DR SMR; Q9ZE56; -.
DR STRING; 272947.RP091; -.
DR EnsemblBacteria; CAA14561; CAA14561; CAA14561.
DR GeneID; 57569218; -.
DR KEGG; rpr:RP091; -.
DR PATRIC; fig|272947.5.peg.91; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_5; -.
DR Proteomes; UP000002480; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..399
FT /note="Probable aspartate/prephenate aminotransferase"
FT /id="PRO_0000123851"
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; 44282 MW; 5E45B9830AC0A511 CRC64;
MSIISTRLNS IKPSPTLAVV KKTLELKKAG VNIIALGAGE PDFDTPDNIK EVAITSIKDG
FTKYTNVDGI PLLKQAIKNK FKRENNIDYE LDEIIVSTGG KQVIYNLFMA SLDKGDEVII
PVPYWVSYPD MVALSTGTPV FVNCGIENNF KLSVEALEHS ITDKTKWLII NSPSNPTGAG
YNCKELENIA KTLRKYPNVN IMSDDIYEHI TFDDFKFYTL AQIAPDLKER IFTVNGVSKA
YSMTGWRIGY GAGSKALIKA MTIIQSQSTS NPCSISQMAA IEALNGTQDY IKSNALNFQK
KRDLALSILE EVTYFECYKP EGAFYLFVKC DKIFGTKTKS GRIIANSNNF SEYLLEEAKV
AVVPGIAFGL DGYFRISYAT SMQELEEACI RIKHACNAL
