ID A0A0Q5PCM5_9BURK Unreviewed; 406 AA.
AC A0A0Q5PCM5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Serine--glyoxylate aminotransferase {ECO:0000313|EMBL:KQR79021.1};
GN ORFNames=ASG35_10720 {ECO:0000313|EMBL:KQR79021.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR79021.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR79021.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR79021.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR79021.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR79021.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQR79021.1}.
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DR EMBL; LMPF01000021; KQR79021.1; -; Genomic_DNA.
DR RefSeq; WP_056360940.1; NZ_LMPF01000021.1.
DR AlphaFoldDB; A0A0Q5PCM5; -.
DR OrthoDB; 9766472at2; -.
DR Proteomes; UP000051826; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KQR79021.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Transferase {ECO:0000313|EMBL:KQR79021.1}.
FT DOMAIN 48..297
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 206
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 406 AA; 43635 MW; 9BAAE272C1CDF3B3 CRC64;
MLKLDFHPAG RHFLQIPGPS PVPDRILRAM SYPTIDHRGP EFGALGLKVL EGIRSIFKTA
QPVVIYPASG TGAWEAALCN TLSPGDTVLM FETGHFATLW KKMAENLGLK PEFLGLPGTE
GWRRGVQADM IEARLREDTE HKIKAVCVVH NETSTGVTSD IASVRRAIDA AGHPALFLVD
TISGLASADY RHDEWGVDVT VSGSQKGLML PPGISFNAVS KKAIEASKSA KLPRAFWAWD
EIIEMNKSGY WPYTPNTNLL YGLSEALEMI GDEGLDNVFA RHQRLAAACR AAVNAWGLEI
QCADPAVYSP VLTGVMTPEG VDADALRKLI YEKFDMSLGT GLGKLKGRMF RIGHLGDCND
LTLMATLTGC EMGLKLAGVK LAGSGVLAAM DYLTSNVAAP ALKAAA
//
