ID A0A0K8P2G3_IDESA Unreviewed; 400 AA.
AC A0A0K8P2G3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine--glyoxylate aminotransferase {ECO:0000313|EMBL:GAP36719.1};
DE EC=2.6.1.45 {ECO:0000313|EMBL:GAP36719.1};
GN ORFNames=ISF6_2559 {ECO:0000313|EMBL:GAP36719.1};
OS Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Piscinibacter.
OX NCBI_TaxID=1547922 {ECO:0000313|EMBL:GAP36719.1, ECO:0000313|Proteomes:UP000037660};
RN [1] {ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "Discovery of a poly(ethylene terephthalate assimilation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP36719.1, ECO:0000313|Proteomes:UP000037660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110686 / TISTR 2288 / 201-F6
RC {ECO:0000313|Proteomes:UP000037660};
RX PubMed=26965627; DOI=10.1126/science.aad6359;
RA Yoshida S., Hiraga K., Takehana T., Taniguchi I., Yamaji H., Maeda Y.,
RA Toyohara K., Miyamoto K., Kimura Y., Oda K.;
RT "A bacterium that degrades and assimilates poly(ethylene terephthalate).";
RL Science 351:1196-1199(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAP36719.1}.
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DR EMBL; BBYR01000038; GAP36719.1; -; Genomic_DNA.
DR RefSeq; WP_054020703.1; NZ_BBYR01000038.1.
DR AlphaFoldDB; A0A0K8P2G3; -.
DR STRING; 1547922.ISF6_2559; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000037660; Unassembled WGS sequence.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR CDD; cd06451; AGAT_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; IPR000192; Aminotrans_V_dom.
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:SF24; ALANINE--GLYOXYLATE AMINOTRANSFERASE 1; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:GAP36719.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000037660};
KW Transferase {ECO:0000313|EMBL:GAP36719.1}.
FT DOMAIN 27..307
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 400 AA; 43265 MW; 0A987E62E1B25A4C CRC64;
MAGRNGLFVP GPTNVPDRVL RAMVVPMEDH RSPRFPALTR DCLEGLKAVF KTSTATPFLF
PSSGTGCWEA ALSNCLSPGD MVLVARFGQF SHLWVDMCHR LGFEVQVLEC EWGEGAPLER
YEAALAADTA HRIKAVLVTH NETATGVTSD VAGVRRAMDA TGHPALLFVD AVSSLASIDF
RMDDWKVDVC VSGSQKGLMM PAGLGVTCVS EKALEARRRT ARQPVCYFDY IDMQNQNRNG
YFPYTPPLPL LYGLRESLAM LAEEGLENVF RRHAYLAGGV RAAVQQGWGL EVCAKQPQWY
SDTVSAVVVP AGTDAARVID RAFRRYNLSL GAGLSKVAGK VFRIGHLGDC NELMLMQAIG
GAEMAMIDCG LPIEPGSGVA AAQRHWRAHE AEASGTTGGM
//
