ID A0A160FP22_9BURK Unreviewed; 409 AA.
AC A0A160FP22;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alanine--glyoxylate aminotransferase {ECO:0000313|EMBL:ANB74515.1};
GN ORFNames=AYM40_02740 {ECO:0000313|EMBL:ANB74515.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB74515.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB74515.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB74515.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP014578; ANB74515.1; -; Genomic_DNA.
DR RefSeq; WP_063497808.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FP22; -.
DR STRING; 1804984.AYM40_02740; -.
DR KEGG; buz:AYM40_02740; -.
DR Proteomes; UP000076852; Chromosome 1.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ANB74515.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Transferase {ECO:0000313|EMBL:ANB74515.1}.
FT DOMAIN 54..351
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 218
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 409 AA; 43474 MW; 3F5C0C3E368BA5C1 CRC64;
MPTSSTSAAP VSYTVPCPVV ESLDAILPEE PLLMMGAGPV PIPAAVAKAN TVVINHLGST
MVKVIGQVKT MARYVFQTNS KWVLGVAGPG SAAMEMAISN LAWEGTKVLS IRNGFFSERM
AEMGRRVGAH VAMLDVEDGT VASLEKVAEA IRRERPEIVT VVQGETSNTV WNHHLKDIAA
LAKAAGALVI VDAVCTLSTM PLEMDAWGID AVITGGQKGL SSIPGVSLIA FSDEAWARVK
GRTAPNAHWC LDASLAENFW HNAGYHYTAP VSGVLALHEA LRLVCAETLE KRFARHLKCS
VALQAGITAL GLQLYAPAPC RLNSVVGIVV PERLSPADIC GHISRHHQVE ISGSFGLPIV
RIGQMGEQCR EHNLFRTLHA LGRTMVDLGV KVELPAGVAA LERGLSEGK
//
