AAPAT_NITEU
ID AAPAT_NITEU Reviewed; 397 AA.
AC Q82WA8;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Name=aatA {ECO:0000312|EMBL:CAD84697.1};
GN OrderedLocusNames=NE0786 {ECO:0000312|EMBL:CAD84697.1};
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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, with lower
CC efficiency (PubMed:24302739). {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=35 uM for oxaloacetate {ECO:0000269|PubMed:24302739};
CC KM=400 uM for prephenate {ECO:0000269|PubMed:24302739};
CC Note=kcat is 33 sec(-1) with oxaloacetate as substrate. kcat is 0.8
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}.
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DR EMBL; AL954747; CAD84697.1; -; Genomic_DNA.
DR RefSeq; WP_011111398.1; NC_004757.1.
DR AlphaFoldDB; Q82WA8; -.
DR SMR; Q82WA8; -.
DR STRING; 228410.NE0786; -.
DR EnsemblBacteria; CAD84697; CAD84697; NE0786.
DR KEGG; neu:NE0786; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_4; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 554560at2; -.
DR PhylomeDB; Q82WA8; -.
DR Proteomes; UP000001416; 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 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..397
FT /note="Aspartate/prephenate aminotransferase"
FT /id="PRO_0000448261"
FT BINDING 38
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P00509"
FT BINDING 124
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT BINDING 174
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 11
FT /note="Important for prephenate aminotransferase activity"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
FT MOD_RES 238
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q56232"
SQ SEQUENCE 397 AA; 42755 MW; 4D4F2CBA7A6E6EBE CRC64;
MKLSQRVQAI KPSPTLAVTA KAARLKAEGK NIIGLGAGEP DFDTPLHIKD AAITAIRNGF
TKYTAVGGTA SLKQAIISKF KRENSLEFMP GEILVSSGGK QSFFNLVLAT IDPGDEVIIP
APYWVSYPDI VLIAEGKPVF IDTGIEEKFK ISPDQLEKAI TPRTRMFVVN SPSNPSGSVY
SLEELQALGA VLRKYPDILI ATDDMYEHIL LSGDGFVNIL NACPDLKART VVLNGVSKAY
AMTGWRIGYC GGPAAIITAM ENIQSQSTSN PNSIAQVAAE AALNGDQSCM VPMIEAFRER
NQFLTNALNS IAGIHCLLSE GAFYAFVDVR QAISRLNTQQ ILQNSSDIAF CNYVLEKAEV
AAVPGSAFGC EGYMRLSFAT SMDNLQEAVK RIASLLS
