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   12-OCT-2022, entry version 41.
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}.
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   AlphaFoldDB; P84188; -.
DR   SMR; 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
//