ID AAT_RICTY Reviewed; 399 AA. AC Q68XV9; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 29-OCT-2014, entry version 61. DE RecName: Full=Aspartate aminotransferase; DE Short=AspAT; DE EC=2.6.1.1; 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., RA Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., RA Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., RA Gibbs R.A., Hong C., Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with RT sequences of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate + CC L-glutamate. CC -!- COFACTOR: Pyridoxal phosphate. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. 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; YP_067015.1; NC_006142.1. DR ProteinModelPortal; Q68XV9; -. DR STRING; 257363.RT0046; -. DR EnsemblBacteria; AAU03533; AAU03533; RT0046. DR GeneID; 2958751; -. DR KEGG; rty:RT0046; -. DR PATRIC; 17909242; VBIRicTyp34752_0043. DR eggNOG; COG0436; -. DR HOGENOM; HOG000223062; -. DR KO; K00812; -. DR OMA; QVEPQLY; -. DR OrthoDB; EOG6RRKNS; -. DR BioCyc; RTYP257363:GJEQ-48-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0080130; F:L-phenylalanine: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; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. 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; Complete proteome; Cytoplasm; Pyridoxal phosphate; KW Transferase. FT CHAIN 1 399 Aspartate aminotransferase. FT /FTId=PRO_0000273126. FT BINDING 39 39 Aspartate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 125 125 Aspartate. {ECO:0000250}. FT BINDING 175 175 Aspartate. {ECO:0000250}. FT BINDING 375 375 Aspartate. {ECO:0000250}. FT MOD_RES 239 239 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. 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 //