AAPAT_THET8
ID AAPAT_THET8 Reviewed; 385 AA.
AC Q56232; Q5SM97;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Aspartate/prephenate aminotransferase {ECO:0000305};
DE Short=AspAT / PAT {ECO:0000305};
DE EC=2.6.1.1 {ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:8907187};
DE EC=2.6.1.78 {ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:30771275};
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=TTHA0046;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=8907187; DOI=10.1093/oxfordjournals.jbchem.a021198;
RA Okamoto A., Kato R., Masui R., Yamagishi A., Oshima T., Kuramitsu S.;
RT "An aspartate aminotransferase from an extremely thermophilic bacterium,
RT Thermus thermophilus HB8.";
RL J. Biochem. 119:135-144(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25070637; DOI=10.1105/tpc.114.127407;
RA Dornfeld C., Weisberg A.J., Ritesh K.C., Dudareva N., Jelesko J.G.,
RA Maeda H.A.;
RT "Phylobiochemical characterization of class-Ib aspartate/prephenate
RT aminotransferases reveals evolution of the plant arogenate phenylalanine
RT pathway.";
RL Plant Cell 26:3101-3114(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LYS-12.
RX PubMed=30771275; DOI=10.1111/febs.14789;
RA Giustini C., Graindorge M., Cobessi D., Crouzy S., Robin A., Curien G.,
RA Matringe M.;
RT "Tyrosine metabolism: identification of a key residue in the acquisition of
RT prephenate aminotransferase activity by 1beta aspartate aminotransferase.";
RL FEBS J. 286:2118-2134(2019).
RN [5] {ECO:0007744|PDB:1BJW, ECO:0007744|PDB:1BKG}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MALEIC ACID AND
RP PYRIDOXAL PHOSPHATE, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=10029535; DOI=10.1021/bi9819881;
RA Nakai T., Okada K., Akutsu S., Miyahara I., Kawaguchi S., Kato R.,
RA Kuramitsu S., Hirotsu K.;
RT "Structure of Thermus thermophilus HB8 aspartate aminotransferase and its
RT complex with maleate.";
RL Biochemistry 38:2413-2424(1999).
RN [6] {ECO:0007744|PDB:1B5O, ECO:0007744|PDB:1B5P, ECO:0007744|PDB:1GC3, ECO:0007744|PDB:1GC4, ECO:0007744|PDB:1GCK, ECO:0007744|PDB:5BJ3, ECO:0007744|PDB:5BJ4}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE
RP AND ASPARTATE, COFACTOR, AND SUBUNIT.
RX PubMed=11432784; DOI=10.1093/oxfordjournals.jbchem.a002966;
RA Ura H., Nakai T., Kawaguchi S., Miyahara I., Hirotsu K., Kuramitsu S.;
RT "Substrate recognition mechanism of thermophilic dual-substrate enzyme.";
RL J. Biochem. 130:89-98(2001).
CC -!- FUNCTION: Catalyzes the reversible conversion of aspartate and 2-
CC oxoglutarate to glutamate and oxaloacetate (PubMed:8907187,
CC PubMed:25070637). Can also transaminate prephenate in the presence of
CC aspartate (PubMed:25070637, PubMed:30771275).
CC {ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:30771275,
CC ECO:0000269|PubMed:8907187}.
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:25070637, ECO:0000269|PubMed:8907187};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate;
CC Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78;
CC Evidence={ECO:0000269|PubMed:25070637, ECO:0000269|PubMed:30771275};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11432784, ECO:0000269|PubMed:8907187};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for L-aspartate (at 45 degrees Celsius)
CC {ECO:0000269|PubMed:8907187};
CC KM=1.0 mM for 2-oxoglutarate (at 45 degrees Celsius)
CC {ECO:0000269|PubMed:8907187};
CC KM=150 uM for prephenate {ECO:0000269|PubMed:30771275};
CC KM=25.3 uM for oxaloacetate {ECO:0000269|PubMed:30771275};
CC Note=kcat is 7.7 sec(-1) toward prephenate. kcat is 32.2 sec(-1)
CC toward oxaloacetate. {ECO:0000269|PubMed:30771275};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10029535,
CC ECO:0000269|PubMed:11432784}.
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; D38459; BAA07487.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69869.1; -; Genomic_DNA.
DR RefSeq; WP_011227669.1; NC_006461.1.
DR RefSeq; YP_143312.1; NC_006461.1.
DR PDB; 1B5O; X-ray; 2.20 A; A/B=1-385.
DR PDB; 1B5P; X-ray; 1.80 A; A/B=1-385.
DR PDB; 1BJW; X-ray; 1.80 A; A/B=1-382.
DR PDB; 1BKG; X-ray; 2.60 A; A/B/C/D=1-385.
DR PDB; 1GC3; X-ray; 3.30 A; A/B/C/D/E/F/G/H=1-385.
DR PDB; 1GC4; X-ray; 3.30 A; A/B/C/D=1-385.
DR PDB; 1GCK; X-ray; 2.50 A; A/B=1-385.
DR PDB; 5BJ3; X-ray; 2.20 A; A/B/C/D=1-385.
DR PDB; 5BJ4; X-ray; 2.00 A; A/B=1-385.
DR PDBsum; 1B5O; -.
DR PDBsum; 1B5P; -.
DR PDBsum; 1BJW; -.
DR PDBsum; 1BKG; -.
DR PDBsum; 1GC3; -.
DR PDBsum; 1GC4; -.
DR PDBsum; 1GCK; -.
DR PDBsum; 5BJ3; -.
DR PDBsum; 5BJ4; -.
DR AlphaFoldDB; Q56232; -.
DR SMR; Q56232; -.
DR STRING; 300852.55771428; -.
DR DrugBank; DB04299; Maleic acid.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR EnsemblBacteria; BAD69869; BAD69869; BAD69869.
DR GeneID; 3168657; -.
DR KEGG; ttj:TTHA0046; -.
DR PATRIC; fig|300852.9.peg.44; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_0; -.
DR OMA; IHMEVGQ; -.
DR PhylomeDB; Q56232; -.
DR BRENDA; 2.6.1.1; 2305.
DR BRENDA; 2.6.1.78; 2305.
DR EvolutionaryTrace; Q56232; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033853; F:aspartate-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; 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 3D-structure; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..385
FT /note="Aspartate/prephenate aminotransferase"
FT /id="PRO_0000123856"
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:0007744|PDB:1GCK"
FT BINDING 175
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0007744|PDB:1GCK"
FT BINDING 361
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0007744|PDB:1GCK"
FT SITE 12
FT /note="Important for prephenate aminotransferase activity"
FT /evidence="ECO:0000269|PubMed:30771275"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:10029535,
FT ECO:0000269|PubMed:11432784, ECO:0007744|PDB:1B5O,
FT ECO:0007744|PDB:1B5P, ECO:0007744|PDB:5BJ3,
FT ECO:0007744|PDB:5BJ4"
FT MUTAGEN 12
FT /note="K->G: 10-fold increase in Km for prephenate. Does
FT not affect Km for oxaloacetate."
FT /evidence="ECO:0000269|PubMed:30771275"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:1B5P"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:1B5P"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1B5P"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:1B5P"
FT TURN 233..237
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:1B5P"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1BJW"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 282..310
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:1B5P"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1B5P"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 368..377
FT /evidence="ECO:0007829|PDB:1B5P"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:1B5P"
SQ SEQUENCE 385 AA; 42051 MW; EADF7B7EA127F39B CRC64;
MRGLSRRVQA MKPSATVAVN AKALELRRQG VDLVALTAGE PDFDTPEHVK EAARRALAQG
KTKYAPPAGI PELREALAEK FRRENGLSVT PEETIVTVGG KQALFNLFQA ILDPGDEVIV
LSPYWVSYPE MVRFAGGVVV EVETLPEEGF VPDPERVRRA ITPRTKALVV NSPNNPTGAV
YPKEVLEALA RLAVEHDFYL VSDEIYEHLL YEGEHFSPGR VAPEHTLTVN GAAKAFAMTG
WRIGYACGPK EVIKAMASVS SQSTTSPDTI AQWATLEALT NQEASRAFVE MAREAYRRRR
DLLLEGLTAL GLKAVRPSGA FYVLMDTSPI APDEVRAAER LLEAGVAVVP GTDFAAFGHV
RLSYATSEEN LRKALERFAR VLGRA
