TYRB_PARDE
ID TYRB_PARDE Reviewed; 394 AA.
AC P95468;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Aromatic-amino-acid aminotransferase;
DE Short=ARAT;
DE Short=AROAT;
DE EC=2.6.1.57;
GN Name=tyrB;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBRC 12442;
RX PubMed=9058208; DOI=10.1093/oxfordjournals.jbchem.a021561;
RA Oue S., Okamoto A., Nakai Y., Nakahira M., Shibatani T., Hayashi H.,
RA Kagamiyama H.;
RT "Paracoccus denitrificans aromatic amino acid aminotransferase: a model
RT enzyme for the study of dual substrate recognition mechanism.";
RL J. Biochem. 121:161-171(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL
RP PHOSPHATE AND SUBSTRATE ANALOGS, AND SUBUNIT.
RX PubMed=9665848; DOI=10.1006/jmbi.1998.1869;
RA Okamoto A., Nakai Y., Hayashi H., Hirotsu K., Kagamiyama H.;
RT "Crystal structures of Paracoccus denitrificans aromatic amino acid
RT aminotransferase: a substrate recognition site constructed by rearrangement
RT of hydrogen bond network.";
RL J. Mol. Biol. 280:443-461(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL PHOSPHATE
RP AND SUBSTRATE ANALOGS, AND PYRIDOXAL PHOSPHATE AT LYS-243.
RX PubMed=9930977; DOI=10.1021/bi981921d;
RA Okamoto A., Ishii S., Hirotsu K., Kagamiyama H.;
RT "The active site of Paracoccus denitrificans aromatic amino acid
RT aminotransferase has contrary properties: flexibility and rigidity.";
RL Biochemistry 38:1176-1184(1999).
CC -!- FUNCTION: Shows activities toward both dicarboxylic and aromatic
CC substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic
CC oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9665848}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Y08272; CAA69597.1; -; Genomic_DNA.
DR PIR; JC5197; JC5197.
DR RefSeq; WP_011746975.1; NZ_PPGA01000002.1.
DR PDB; 1AY4; X-ray; 2.33 A; A/B=1-394.
DR PDB; 1AY5; X-ray; 2.50 A; A/B=1-394.
DR PDB; 1AY8; X-ray; 2.30 A; A/B=1-394.
DR PDB; 2AY1; X-ray; 2.20 A; A/B=1-394.
DR PDB; 2AY2; X-ray; 2.40 A; A/B=1-394.
DR PDB; 2AY3; X-ray; 2.40 A; A/B=1-394.
DR PDB; 2AY4; X-ray; 2.20 A; A/B=1-394.
DR PDB; 2AY5; X-ray; 2.40 A; A/B=1-394.
DR PDB; 2AY6; X-ray; 2.20 A; A/B=1-394.
DR PDB; 2AY7; X-ray; 2.40 A; A/B=1-394.
DR PDB; 2AY8; X-ray; 2.20 A; A/B=1-394.
DR PDB; 2AY9; X-ray; 2.50 A; A/B=1-394.
DR PDBsum; 1AY4; -.
DR PDBsum; 1AY5; -.
DR PDBsum; 1AY8; -.
DR PDBsum; 2AY1; -.
DR PDBsum; 2AY2; -.
DR PDBsum; 2AY3; -.
DR PDBsum; 2AY4; -.
DR PDBsum; 2AY5; -.
DR PDBsum; 2AY6; -.
DR PDBsum; 2AY7; -.
DR PDBsum; 2AY8; -.
DR PDBsum; 2AY9; -.
DR AlphaFoldDB; P95468; -.
DR SMR; P95468; -.
DR DrugBank; DB04208; 3-(3,4-dimethoxyphenyl)propanoic acid.
DR DrugBank; DB03400; 3-(P-Tolyl)Propionic Acid.
DR DrugBank; DB02740; 3-Indolebutyric Acid.
DR DrugBank; DB02024; 3-phenylpropionic acid.
DR DrugBank; DB02434; 4-(2-Thienyl)Butyric Acid.
DR DrugBank; DB03210; 4-Aminohydrocinnamic Acid.
DR DrugBank; DB04051; 5-phenylpentanoic acid.
DR DrugBank; DB02242; Cyclohexanepropanoic acid.
DR DrugBank; DB02758; Indolepropionic acid.
DR DrugBank; DB04299; Maleic acid.
DR DrugBank; DB06819; Phenylbutyric acid.
DR OMA; PTWPIHE; -.
DR BRENDA; 2.6.1.57; 3341.
DR EvolutionaryTrace; P95468; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Aromatic amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..394
FT /note="Aromatic-amino-acid aminotransferase"
FT /id="PRO_0000123894"
FT BINDING 34
FT /ligand="substrate"
FT BINDING 65
FT /ligand="substrate"
FT BINDING 127
FT /ligand="substrate"
FT BINDING 180
FT /ligand="substrate"
FT BINDING 371
FT /ligand="substrate"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2AY1"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:2AY1"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 218..231
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:2AY1"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 298..330
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2AY9"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 343..347
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:2AY1"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:2AY1"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:2AY1"
FT HELIX 382..392
FT /evidence="ECO:0007829|PDB:2AY1"
SQ SEQUENCE 394 AA; 42732 MW; 092FC4643F1E387A CRC64;
MLGNLKPQAP DKILALMGEF RADPRQGKID LGVGVYKDAT GHTPIMRAVH AAEQRMLETE
TTKTYAGLSG EPEFQKAMGE LILGDGLKSE TTATLATVGG TGALRQALEL ARMANPDLRV
FVSDPTWPNH VSIMNFMGLP VQTYRYFDAE TRGVDFEGMK ADLAAAKKGD MVLLHGCCHN
PTGANLTLDQ WAEIASILEK TGALPLIDLA YQGFGDGLEE DAAGTRLIAS RIPEVLIAAS
CSKNFGIYRE RTGCLLALCA DAATRELAQG AMAFLNRQTY SFPPFHGAKI VSTVLTTPEL
RADWMAELEA VRSGMLRLRE QLAGELRDLS GSDRFGFVAE HRGMFSRLGA TPEQVKRIKE
EFGIYMVGDS RINIAGLNDN TIPILARAII EVGV
