ID   D0VX02_9FIRM            Unreviewed;       398 AA.
AC   D0VX02;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=RER070207001803 {ECO:0000313|PDB:3ELE};
OS   Agathobacter rectalis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Agathobacter.
OX   NCBI_TaxID=39491 {ECO:0000313|PDB:3ELE};
RN   [1] {ECO:0000313|PDB:3ELE, ECO:0007829|PDB:3ELE}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH
RP   N6-(PYRIDOXALPHOSPHATE)LYSINE.
RG   Joint Center for Structural Genomics (JCSG);
RT   "Crystal structure of Amino Transferase (RER070207001803) from Eubacterium
RT   rectale at 2.10 A resolution.";
RL   Submitted (SEP-2008) to the PDB data bank.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR   PDB; 3ELE; X-ray; 2.10 A; A/B/C/D=1-398.
DR   PDBsum; 3ELE; -.
DR   AlphaFoldDB; D0VX02; -.
DR   SMR; D0VX02; -.
DR   EvolutionaryTrace; D0VX02; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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; 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   PANTHER; PTHR42691; ASPARTATE AMINOTRANSFERASE YHDR-RELATED; 1.
DR   PANTHER; PTHR42691:SF1; ASPARTATE AMINOTRANSFERASE YHDR-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000313|PDB:3ELE, ECO:0007829|PDB:3ELE};
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481};
KW   Transferase {ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          36..384
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   BINDING         72
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         108
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         109
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         134
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         183
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         245
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         247
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         248
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
FT   BINDING         256
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0007829|PDB:3ELE"
SQ   SEQUENCE   398 AA;  44448 MW;  BF4A60C9277B6FAD CRC64;
     GMVVNESMYQ LGSVRSAIRE LFEYGKKRAA IVGKENVYDF SIGNPSIPAP QIVNDTIKEL
     VTDYDSVALH GYTSAQGDVE TRAAIAEFLN NTHGTHFNAD NLYMTMGAAA SLSICFRALT
     SDAYDEFITI APYFPEYKVF VNAAGARLVE VPADTEHFQI DFDALEERIN AHTRGVIINS
     PNNPSGTVYS EETIKKLSDL LEKKSKEIGR PIFIIADEPY REIVYDGIKV PFVTKYYDNT
     LVCYSYSKSL SLPGERIGYV LVPDEVYDKA ELYAAVCGAG RALGYVCAPS LFQKMIVKCQ
     GATGDINAYK ENRDLLYEGL TRIGYHCFKP DGAFYMFVKA LEDDSNAFCE KAKEEDVLIV
     AADGFGCPGW VRISYCVDRE MIKHSMPAFE KIYKKYNK
//