AAPAT_RICBR
ID AAPAT_RICBR Reviewed; 399 AA.
AC Q1RGV0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=RBE_1333;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05414.1; -; Genomic_DNA.
DR RefSeq; WP_011477983.1; NC_007940.1.
DR AlphaFoldDB; Q1RGV0; -.
DR SMR; Q1RGV0; -.
DR STRING; 336407.RBE_1333; -.
DR EnsemblBacteria; ABE05414; ABE05414; RBE_1333.
DR KEGG; rbe:RBE_1333; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 554560at2; -.
DR Proteomes; UP000001951; 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..399
FT /note="Probable aspartate/prephenate aminotransferase"
FT /id="PRO_0000273124"
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; 43981 MW; 09F007EFF3ABCE9A CRC64;
MSIISTQLNA IKPSPTLAVV RKTLELKRAG IDIIALGAGE PDFDTPDNIK EAAIKAIKDG
FTKYTNVEGI PALKEAIQAK FKRENNIDYD LEEIIVSTGG KQVIYNLFMA SLNKGDEVII
PAPYWVSYPD MVLLAEGTPV FANCGIESNF KLSGEALEQL ITPKTKWLII NSPSNPTGAS
YSHSELKNIA EVLRKHPYVN VMSDDIYEHI TFDGFKFYTL AEIAPDLKDR IFTVNGVSKA
YSMTGWRIGY GAGSKALIKA MTIIQSQSTS NPCSISQVAA VEALNGVQGY IAQNALNFEK
KRDLALSILQ RVKYFECYKP EGAFYLFIKC DKIFGAKTKS GKVINNSNDF GEYLLEEAKV
AVVPGIAFGL EGYFRISYAT SMEELEEACL RMERACGSL
