AAPAT_CERS1
ID AAPAT_CERS1 Reviewed; 400 AA.
AC A3PMF8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Aspartate/prephenate aminotransferase {ECO:0000305};
DE Short=AspAT / PAT {ECO:0000305};
DE EC=2.6.1.1 {ECO:0000269|PubMed:24302739};
DE EC=2.6.1.79 {ECO:0000269|PubMed:24302739};
GN OrderedLocusNames=Rsph17029_2422 {ECO:0000312|EMBL:ABN77524.1};
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=RCR2011;
RX PubMed=24302739; DOI=10.1074/jbc.m113.486480;
RA Graindorge M., Giustini C., Kraut A., Moyet L., Curien G., Matringe M.;
RT "Three different classes of aminotransferases evolved prephenate
RT aminotransferase functionality in arogenate-competent microorganisms.";
RL J. Biol. Chem. 289:3198-3208(2014).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate (PubMed:24302739). Can also
CC transaminate prephenate in the presence of glutamate (PubMed:24302739).
CC {ECO:0000269|PubMed:24302739}.
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:0000269|PubMed:24302739};
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:0000269|PubMed:24302739};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q56232};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27 uM for oxaloacetate {ECO:0000269|PubMed:24302739};
CC KM=290 uM for prephenate {ECO:0000269|PubMed:24302739};
CC Note=kcat is 150 sec(-1) with oxaloacetate as substrate. kcat is 56
CC sec(-1) with prephenate as substrate. {ECO:0000269|PubMed:24302739};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q56232}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; CP000577; ABN77524.1; -; Genomic_DNA.
DR RefSeq; WP_002720951.1; NC_009049.1.
DR AlphaFoldDB; A3PMF8; -.
DR SMR; A3PMF8; -.
DR EnsemblBacteria; ABN77524; ABN77524; Rsph17029_2422.
DR GeneID; 57471093; -.
DR KEGG; rsh:Rsph17029_2422; -.
DR HOGENOM; CLU_017584_4_3_5; -.
DR OMA; APYWTTY; -.
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; 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.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT CHAIN 1..400
FT /note="Aspartate/prephenate aminotransferase"
FT /id="PRO_0000448262"
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 400 AA; 42861 MW; 64ECD119CD337CA9 CRC64;
MAFLSDTLAR VKPSQTIAVT NKARELAAAG RDVIGLGAGE PDFDTPDNIK AAAKRAIDAG
RTKYTAVDGI PELKRAICEK FERENGLKYT PAQVTVGTGG KQILYNALVA TLNPGDEVII
PAPYWVSYPD MVLLAGGTPV SVAAGMETGF KLTPEQLEAA ITPRTKWFIF NSPSNPTGAA
YTRAELAALC EVLMRHPQVW IMSDDMYEHL VFDDFDFTTP AQIEPGLYDR TLTCNGVSKA
YCMTGWRIGY AAGPVELIRA MGTIQSQSTS NPCSIAQYAA LEALSGPQEF LATNREAFQR
RRDLVVSMLN EAKGVTCPNP EGAFYVYPDI SGCIGKTSAG GAKITDDEAF ASALLEETGV
AVVFGAAFGL SPNFRISYAT ADEVLREACA RIQAFCAGLS
