ID   F2XBU9_VIBFL            Unreviewed;       453 AA.
AC   F2XBU9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Pyruvate transaminase {ECO:0000313|EMBL:AEA39183.1};
OS   Vibrio fluvialis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=676 {ECO:0000313|EMBL:AEA39183.1};
RN   [1] {ECO:0000313|EMBL:AEA39183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JS17 {ECO:0000313|EMBL:AEA39183.1};
RX   PubMed=12687298;
RA   Shin J.S., Yun H., Jang J.W., Park I., Kim B.G.;
RT   "Purification, characterization, and molecular cloning of a novel
RT   amine:pyruvate transaminase from Vibrio fluvialis JS17.";
RL   Appl. Microbiol. Biotechnol. 61:463-471(2003).
RN   [2] {ECO:0007829|PDB:3NUI}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA   Park H.H., Jang T.;
RT   "Crystal structure of the first omega-transaminase at 2.0A resolution.";
RL   Submitted (JUL-2010) to the PDB data bank.
RN   [3] {ECO:0000313|EMBL:AEA39183.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JS17 {ECO:0000313|EMBL:AEA39183.1};
RA   Shin J.-S., Yun H., Jang J.-W., Park I., Kim B.-G.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0007829|PDB:4E3Q, ECO:0007829|PDB:4E3R}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND PYRIDOXAL PHOSPHATE AT GLY-117;
RP   SER-118 AND THR-322.
RX   PubMed=23012440; DOI=10.1093/protein/gzs065;
RA   Midelfort K.S., Kumar R., Han S., Karmilowicz M.J., McConnell K.,
RA   Gehlhaar D.K., Mistry A., Chang J.S., Anderson M., Villalobos A.,
RA   Minshull J., Govindarajan S., Wong J.W.;
RT   "Redesigning and characterizing the substrate specificity and activity of
RT   Vibrio fluvialis aminotransferase for the synthesis of imagabalin.";
RL   Protein Eng. Des. Sel. 26:25-33(2013).
RN   [5] {ECO:0007829|PDB:5ZTX}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RX   PubMed=30061559; DOI=10.1038/s41598-018-29846-0;
RA   Shin Y.C., Yun H., Park H.H.;
RT   "Structural dynamics of the transaminase active site revealed by the
RT   crystal structure of a co-factor free omega-transaminase from Vibrio
RT   fluvialis JS17.";
RL   Sci. Rep. 8:11454-11454(2018).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; HQ418483; AEA39183.1; -; Genomic_DNA.
DR   PDB; 3NUI; X-ray; 2.00 A; A/B=1-453.
DR   PDB; 4E3Q; X-ray; 1.90 A; A/B/C/D=1-453.
DR   PDB; 4E3R; X-ray; 1.90 A; A/B/C/D=1-453.
DR   PDB; 5ZTX; X-ray; 2.00 A; A/B=1-453.
DR   PDBsum; 3NUI; -.
DR   PDBsum; 4E3Q; -.
DR   PDBsum; 4E3R; -.
DR   PDBsum; 5ZTX; -.
DR   AlphaFoldDB; F2XBU9; -.
DR   SMR; F2XBU9; -.
DR   BioCyc; MetaCyc:MONOMER-17645; -.
DR   BRENDA; 2.6.1.116; 7901.
DR   EvolutionaryTrace; F2XBU9; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42684:SF3; GAMMA-AMINOBUTYRATE TRANSAMINASE POP2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3NUI, ECO:0007829|PDB:4E3Q};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:AEA39183.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   MOD_RES         117
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0007829|PDB:4E3Q"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0007829|PDB:4E3Q"
FT   MOD_RES         322
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0007829|PDB:4E3Q"
SQ   SEQUENCE   453 AA;  50131 MW;  882C67989E909154 CRC64;
     MNKPQSWEAR AETYSLYGFT DMPSLHQRGT VVVTHGEGPY IVDVNGRRYL DANSGLWNMV
     AGFDHKGLID AAKAQYERFP GYHAFFGRMS DQTVMLSEKL VEVSPFDSGR VFYTNSGSEA
     NDTMVKMLWF LHAAEGKPQK RKILTRWNAY HGVTAVSASM TGKPYNSVFG LPLPGFVHLT
     CPHYWRYGEE GETEEQFVAR LARELEETIQ REGADTIAGF FAEPVMGAGG VIPPAKGYFQ
     AILPILRKYD IPVISDEVIC GFGRTGNTWG CVTYDFTPDA IISSKNLTAG FFPMGAVILG
     PELSKRLETA IEAIEEFPHG FTASGHPVGC AIALKAIDVV MNEGLAENVR RLAPRFEERL
     KHIAERPNIG EYRGIGFMWA LEAVKDKASK TPFDGNLSVS ERIANTCTDL GLICRPLGQS
     VVLCPPFILT EAQMDEMFDK LEKALDKVFA EVA
//