SGAT_WHEAT
ID SGAT_WHEAT Reviewed; 78 AA.
AC P84188;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Serine--glyoxylate aminotransferase;
DE Short=SGAT;
DE EC=2.6.1.45;
DE AltName: Full=Alanine--glyoxylate aminotransferase;
DE Short=AGT;
DE EC=2.6.1.44;
DE Flags: Fragments;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Jasna; TISSUE=Leaf;
RX PubMed=15940352;
RA Truszkiewicz W., Paszkowski A.;
RT "Some structural properties of plant serine:glyoxylate aminotransferase.";
RL Acta Biochim. Pol. 52:527-534(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-serine = 3-hydroxypyruvate + glycine;
CC Xref=Rhea:RHEA:19125, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305; EC=2.6.1.45;
CC Evidence={ECO:0000269|PubMed:15940352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-alanine = glycine + pyruvate;
CC Xref=Rhea:RHEA:24248, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57972; EC=2.6.1.44;
CC Evidence={ECO:0000269|PubMed:15940352};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15940352};
CC -!- ACTIVITY REGULATION: Inhibited by aminooxyacetate.
CC {ECO:0000269|PubMed:15940352}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15940352}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15940352}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves but not in root tissue or
CC seedlings. {ECO:0000269|PubMed:15940352}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:15940352}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255}.
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DR AlphaFoldDB; P84188; -.
DR SMR; P84188; -.
DR PRIDE; P84188; -.
DR Proteomes; UP000019116; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Aminotransferase; Direct protein sequencing; Peroxisome;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN <1..>78
FT /note="Serine--glyoxylate aminotransferase"
FT /id="PRO_0000150236"
FT NON_CONS 16..17
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 24..25
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 38..39
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 44..45
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 54..55
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 58..59
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 63..64
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_CONS 72..73
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:15940352"
FT NON_TER 78
FT /evidence="ECO:0000303|PubMed:15940352"
SQ SEQUENCE 78 AA; 9147 MW; 96F0EB99C741C721 CRC64;
HLFVPGPVNI PDQVLRTLLE DVKKLASRLR SDSQHTIKLL DAYRVFFDWK DYLKKVFRNV
NTLLKDLGYP VKPLIPSR
