ID A4S9U4_OSTLU Unreviewed; 359 AA.
AC A4S9U4;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=alanine--glyoxylate transaminase {ECO:0000256|ARBA:ARBA00013049};
DE EC=2.6.1.44 {ECO:0000256|ARBA:ARBA00013049};
GN ORFNames=OSTLU_18704 {ECO:0000313|EMBL:ABP00444.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABP00444.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABP00444.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABP00444.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
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DR EMBL; CP000597; ABP00444.1; -; Genomic_DNA.
DR RefSeq; XP_001422127.1; XM_001422090.1.
DR AlphaFoldDB; A4S9U4; -.
DR STRING; 436017.A4S9U4; -.
DR EnsemblPlants; ABP00444; ABP00444; OSTLU_18704.
DR GeneID; 5006289; -.
DR Gramene; ABP00444; ABP00444; OSTLU_18704.
DR KEGG; olu:OSTLU_18704; -.
DR eggNOG; KOG2862; Eukaryota.
DR HOGENOM; CLU_044792_0_0_1; -.
DR OMA; QKGWSAS; -.
DR OrthoDB; 34257at2759; -.
DR Proteomes; UP000001568; Chromosome 17.
DR GO; GO:0008453; F:alanine-glyoxylate 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; PTHR42778; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR PANTHER; PTHR42778:SF1; 2-AMINOETHYLPHOSPHONATE--PYRUVATE TRANSAMINASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001568}.
FT DOMAIN 35..261
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 319
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 170
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 359 AA; 38838 MW; DCA63E2C14FAD9D8 CRC64;
MSPVFCETMK NIDGMMKRAY NASGVVIMPG SGTYGMEAVA RQWCSGKKAL VIRNGYFSYR
WTDIFEQTQI PSETIVMRGR AVDDEKTPAF APPPLAEVVE MINKEKPAVV FAPHVETSTG
IILPDSYIKA VADAVHAHGG LFVLDSIASG TIWVDMKATG VDAILSAPQK GWTGPACASV
IMLGERGVHA TRNSQSTSMV INMRKWLEVM DAYLAGGFAY YTTMPTDALT LFERAAMATE
KVGFDKVKQM AWDLGTECRK MMASKGLKSV AAKGFEAPGV VVSYTDDATM FAKFKSKGFQ
IAAGVPFMIN EPAGNNTFRI GLFGLDKIMN KDNCINTLEP TLDEILRENA EAAGAEAAS
//