ID   AGT1_DICDI              Reviewed;         407 AA.
AC   Q54GT6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Serine--pyruvate aminotransferase;
DE            Short=SPT;
DE            EC=2.6.1.51;
DE   AltName: Full=Alanine--glyoxylate aminotransferase;
DE            Short=AGT;
DE            EC=2.6.1.44;
GN   Name=agxt; ORFNames=DDB_G0289923;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Dual metabolic roles of gluconeogenesis and glyoxylate
CC       detoxification. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine;
CC         Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180,
CC         ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51;
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AAFI02000149; EAL62474.1; -; Genomic_DNA.
DR   RefSeq; XP_635983.1; XM_630891.1.
DR   AlphaFoldDB; Q54GT6; -.
DR   SMR; Q54GT6; -.
DR   STRING; 44689.DDB0237978; -.
DR   PaxDb; Q54GT6; -.
DR   EnsemblProtists; EAL62474; EAL62474; DDB_G0289923.
DR   GeneID; 8627398; -.
DR   KEGG; ddi:DDB_G0289923; -.
DR   dictyBase; DDB_G0289923; agxt.
DR   eggNOG; KOG2862; Eukaryota.
DR   HOGENOM; CLU_027686_0_0_1; -.
DR   InParanoid; Q54GT6; -.
DR   OMA; KNWLPIM; -.
DR   PhylomeDB; Q54GT6; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-DDI-9033241; Peroxisomal protein import.
DR   PRO; PR:Q54GT6; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; ISS:dictyBase.
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   GO; GO:0046487; P:glyoxylate metabolic process; ISS:dictyBase.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..407
FT                   /note="Serine--pyruvate aminotransferase"
FT                   /id="PRO_0000328587"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   407 AA;  44711 MW;  D5701FCFDB38DE50 CRC64;
     MGYSDKHKLK TSNLQLPVRL LLGPGPSNLH PRVNQQLISS MVGYTDASYY KVMDETMELM
     RYLFQTDNHF TIPISGAGTA AMETCVSNLI EPGDKVVCLV SGFFSDRIYQ MAVRYGGNIL
     KVDKQWGQWF ALEEIESALV QHKPSLLTLV FGETSTGVKQ QMEGVGELCK KYNCLLMVDC
     VAALGGVPVF VDDWKIDACY TGTQKCLSGP PGISPLTFSN AACHKIATRK TPVANWYLDC
     NLLGGYWCPE FNLADGTIAK EEKSTIPKRY HHTTPANLLY SLREALVLLV EEGLDNVWKR
     HQDAAILLYA GLESLGLKPF VPQLNEAPEK GGRLFSLTTV NIPDGVDGKM VMKYLLDNFN
     IEIAGGIGAF AGKVWRIGLM GQNANPGNIK LLISSLSDAL KVNGFNC