ID A0A0N8K6Y7_9RHOB Unreviewed; 392 AA.
AC A0A0N8K6Y7;
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=Alanine-glyoxylate transaminase / serine-glyoxylate transaminase / serine-pyruvate transaminase {ECO:0000313|EMBL:KPP90249.1};
DE EC=2.6.1.44 {ECO:0000313|EMBL:KPP90249.1};
DE EC=2.6.1.45 {ECO:0000313|EMBL:KPP90249.1};
DE EC=2.6.1.51 {ECO:0000313|EMBL:KPP90249.1};
GN ORFNames=HLUCCA08_15425 {ECO:0000313|EMBL:KPP90249.1};
OS Rhodobacteraceae bacterium HLUCCA08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP90249.1, ECO:0000313|Proteomes:UP000050293};
RN [1] {ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KPP90249.1, ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP90249.1};
RX PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT "Identification and Resolution of Microdiversity through Metagenomic
RT Sequencing of Parallel Consortia.";
RL Appl. Environ. Microbiol. 82:255-267(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:KPP90249.1}.
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DR EMBL; LJSF01000012; KPP90249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8K6Y7; -.
DR STRING; 1666913.HLUCCA08_15425; -.
DR PATRIC; fig|1666913.4.peg.726; -.
DR Proteomes; UP000050293; Unassembled WGS sequence.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004760; F:serine-pyruvate 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:KPP90249.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:KPP90249.1};
KW Transferase {ECO:0000313|EMBL:KPP90249.1}.
FT DOMAIN 70..335
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 392 AA; 41541 MW; 67F7C5BBB4EFB0D9 CRC64;
MFANGRSYLA IPGPSVMPDR VLRAMNRAAP NIYVGELHEV TRSLVPDLKR LAGTTGDLAI
YIANGHGTWE AALANVVAEG DTVLVLATGR FCIGWGEMAA GLGARVETLD FGQAAPVDQA
RVEEALRADT AHRIKAVLSV HVDTSTGVRN DIAALRAAID RAGHPALLMC DTIASLGCDR
YAMDECGADV TVAASQKGLM TPPGLGFVWF NEKADRVRGA MARVSRYWDW RPRANPTEYW
MHFDGTAPTH HVYGLRAALD MIAEEGLEAV WARHDGLARA VWAACGAWGQ GGPLRLNLPD
PAARSRAITS IGMAPGQGDA LRAYLEQRLG VTLGIGLGRD PASAWFRIGH MGHVNAHMVL
GVLAAIETGL RALDIPHGAG ALDAASAVLA AS
//
