ID A0A125NVR7_HYPSL Unreviewed; 397 AA.
AC A0A125NVR7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Serine--glyoxylate aminotransferase {ECO:0000313|EMBL:KWT70618.1};
DE EC=2.6.1.45 {ECO:0000313|EMBL:KWT70618.1};
GN ORFNames=APY04_0898 {ECO:0000313|EMBL:KWT70618.1};
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT70618.1, ECO:0000313|Proteomes:UP000059074};
RN [1] {ECO:0000313|EMBL:KWT70618.1, ECO:0000313|Proteomes:UP000059074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT70618.1,
RC ECO:0000313|Proteomes:UP000059074};
RA Albers P.;
RT "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT consortium.";
RL Submitted (OCT-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:KWT70618.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMTR01000030; KWT70618.1; -; Genomic_DNA.
DR RefSeq; WP_068460068.1; NZ_LMTR01000030.1.
DR AlphaFoldDB; A0A125NVR7; -.
DR STRING; 121290.APY04_0898; -.
DR PATRIC; fig|121290.4.peg.1710; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000059074; Unassembled WGS sequence.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
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:KWT70618.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000059074};
KW Transferase {ECO:0000313|EMBL:KWT70618.1}.
FT DOMAIN 23..318
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 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 397 AA; 42652 MW; 6EA54658EB57F554 CRC64;
MANHAGRHFL QIPGPTPVPE RVHNAMARSM MDHRGPAFCE FGQKLFADVK GIFKTQQPVI
IFPSSGTGSW EAALTNTLSP GDHVLVMETG QFAVLWTKMA ERMGLKPEVI ANDWRSGADA
NALEARLRAD SSQQIKAVCV VQNETSTGAR THIDEIRKAM DAAGHSALLM VDTISSLAAM
DYRHDEWGVD ITISGSQKGL MLPPGLSFTA VSQKALAASK KATLARAYFS WDDMLAINGS
GTFPYTPPIG LLFGLAETIT MLNEEGLSNV FARHERLAEA TRRAVKAWGL EVWCQDARAY
SPVVTAVEMP EGHNSDAFRK IVLENFNMSL GTGLSKLAGK AFRIAHLGYT NELTIMGALA
GVEMGLELAR VPHNKGGVSA AMAYLAQAAS PATAQAA
//
