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 11-DEC-2019, entry version 83. 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; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC 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=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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017197; AAU03533.1; -; Genomic_DNA. DR RefSeq; WP_011190520.1; NC_006142.1. DR SMR; Q68XV9; -. DR STRING; 257363.RT0046; -. DR EnsemblBacteria; AAU03533; AAU03533; RT0046. DR KEGG; rty:RT0046; -. DR eggNOG; ENOG4105CHM; Bacteria. DR eggNOG; COG0436; LUCA. DR HOGENOM; HOG000223062; -. DR KO; K00812; -. DR OMA; SVAMTGW; -. DR OrthoDB; 554560at2; -. DR BioCyc; RTYP257363:G1G0L-47-MONOMER; -. 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: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; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. 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..399 FT /note="Probable aspartate/prephenate aminotransferase" FT /id="PRO_0000273126" FT BINDING 39 FT /note="Aspartate; via amide nitrogen" FT /evidence="ECO:0000250|UniProtKB:P00509" FT BINDING 125 FT /note="Aspartate" FT /evidence="ECO:0000250|UniProtKB:Q56232" FT BINDING 175 FT /note="Aspartate" FT /evidence="ECO:0000250|UniProtKB:Q56232" FT BINDING 375 FT /note="Aspartate" 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 //