ID   SGAT_MAIZE              Reviewed;         136 AA.
AC   P84187;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 61.
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   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Duet; 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; P84187; -.
DR   SMR; P84187; -.
DR   PRIDE; P84187; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P84187; baseline and differential.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IBA:GO_Central.
DR   GO; GO:0050281; F:serine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR   GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Peroxisome;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..>136
FT                   /note="Serine--glyoxylate aminotransferase"
FT                   /id="PRO_0000150235"
FT   NON_CONS        9..10
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        30..31
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        41..42
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        46..47
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        77..78
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        87..88
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        93..94
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        99..100
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        109..110
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_CONS        129..130
FT                   /evidence="ECO:0000303|PubMed:15940352"
FT   NON_TER         136
FT                   /evidence="ECO:0000303|PubMed:15940352"
SQ   SEQUENCE   136 AA;  15039 MW;  78AD53514B68E795 CRC64;
     LDYVYGPGRR AMNSPAVPAL TKVLLEDVKK ALTNTLSPGD RLLLVDMDEW GVDVALTGSQ
     KALSFPTGMG LVCASPRVFF DWKDYLRTYW HYDQALDLEL AVEAWGLSNR YNLSLGLGLN
     KVAGGKVFRD VGYPVK