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-MAY-2023, entry version 119. 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; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; 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}. 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; 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 GeneID; 75500169; -. 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:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd00609; AAT_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; ASPARTATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR11879:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR PRINTS; PR00799; TRANSAMINASE. DR SUPFAM; SSF53383; PLP-dependent transferases; 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 //