ID AGX1_YEAST Reviewed; 385 AA. AC P43567; D6VTK0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-NOV-2026, entry version 185. DE RecName: Full=Alanine--glyoxylate aminotransferase 1 {ECO:0000303|PubMed:3933486}; DE EC=2.6.1.44 {ECO:0000269|PubMed:16226833}; GN Name=AGX1 {ECO:0000303|PubMed:3933486}; OrderedLocusNames=YFL030W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP FUNCTION. RX PubMed=3933486; DOI=10.1042/bj2310157; RA Takada Y., Noguchi T.; RT "Characteristics of alanine:glyoxylate aminotransferase from Saccharomyces RT cerevisiae, a regulatory enzyme in the glyoxylate pathway of glycine and RT serine biosynthesis from tricarboxylic acid-cycle intermediates."; RL Biochem. J. 231:157-163(1985). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [5] RP CHARACTERIZATION. RX PubMed=14745783; DOI=10.1002/yea.1058; RA Schlosser T., Gatgens C., Weber U., Stahmann K.-P.; RT "Alanine:glyoxylate aminotransferase of Saccharomyces cerevisiae-encoding RT gene AGX1 and metabolic significance."; RL Yeast 21:63-73(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PYRODOXAL PHOSPHATE AND GLYOXYLATE, RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DISRUPTION RP PHENOTYPE, FUNCTION, AND SUBUNIT. RX PubMed=16226833; DOI=10.1016/j.biochi.2005.09.001; RA Meyer P., Liger D., Leulliot N., Quevillon-Cheruel S., Zhou C.-Z., RA Borel F., Ferrer J.-L., Poupon A., Janin J., van Tilbeurgh H.; RT "Crystal structure and confirmation of the alanine:glyoxylate RT aminotransferase activity of the YFL030w yeast protein."; RL Biochimie 87:1041-1047(2005). CC -!- FUNCTION: Has alanine:glyoxylate aminotransferase activity. CC {ECO:0000269|PubMed:16226833, ECO:0000269|PubMed:3933486}. 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:16226833}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:16226833}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.26 mM for L-alanine {ECO:0000269|PubMed:16226833}; CC KM=0.18 mM for glyoxylate {ECO:0000269|PubMed:16226833}; CC Vmax=180 umol/min/mg enzyme {ECO:0000269|PubMed:16226833}; CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from CC glyoxylate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16226833}. CC -!- DISRUPTION PHENOTYPE: Alanine:glyoxylate aminotransferase activity is CC reduced by 98% relative to wild-type. {ECO:0000269|PubMed:16226833}. CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium. CC Expression levels higher in stationary phase than in exponential growth CC phase when grown in complex medium with glucose. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. 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 EMBL; D50617; BAA09208.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12410.1; -; Genomic_DNA. DR PIR; S56224; S56224. DR RefSeq; NP_116623.1; NM_001179936.1. DR PDB; 2BKW; X-ray; 2.57 A; A=1-385. DR SMR; P43567; -. DR BioGRID; 31116; 43. DR DIP; DIP-5433N; -. DR IntAct; P43567; 3. DR STRING; 4932.YFL030W; -. DR GlyGen; P43567; 1 site. DR iPTMnet; P43567; -. DR PaxDb; 4932-YFL030W; -. DR PeptideAtlas; P43567; -. DR EnsemblFungi; YFL030W_mRNA; YFL030W; YFL030W. DR GeneID; 850514; -. DR KEGG; sce:YFL030W; -. DR VEuPathDB; FungiDB:YFL030W; -. DR AGR; SGD:S000001864; -. DR SGD; S000001864; AGX1. DR eggNOG; KOG2862; Eukaryota. DR HOGENOM; CLU_027686_5_2_1; -. DR InParanoid; P43567; -. DR OMA; AACAYMQ; -. DR OrthoDB; 7403325at2759; -. DR BioCyc; MetaCyc:MONOMER3O-372; -. DR BioCyc; YEAST:MONOMER3O-372; -. DR BRENDA; 2.6.1.44; 984. DR SABIO-RK; P43567; -. DR UniPathway; UPA00288; UER00428. DR EvolutionaryTrace; P43567; -. DR PRO; PR:P43567; -. DR CDD; cd06451; AGAT_like; 1. DR FunFam; 3.90.1150.10:FF:000049; Alanine-glyoxylate aminotransferase 1; 1. DR FunFam; 3.40.640.10:FF:000027; Serine--pyruvate aminotransferase, mitochondrial; 1. 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; PTHR21152:SF24; ALANINE--GLYOXYLATE AMINOTRANSFERASE 1; 1. DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000524; SPT; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0008453; F:L-alanine:glyoxylate transaminase activity; IDA:SGD. DR GO; GO:0004760; F:L-serine:pyruvate transaminase activity; IBA:GO_Central. DR GO; GO:0006545; P:glycine biosynthetic process; IDA:SGD. DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43567; protein. DR BioGRID-ORCS; 850514; 4 hits in 10 CRISPR screens. DR AlphaFoldDB; P43567; -. DR FunCoup; P43567; 1688. PE 1: Evidence at protein level; KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1..385 FT /note="Alanine--glyoxylate aminotransferase 1" FT /id="PRO_0000150239" FT BINDING 354 FT /ligand="substrate" FT MOD_RES 201 FT /note="N6-(pyridoxal phosphate)lysine" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 18..22 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 34..50 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 70..79 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 96..107 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 126..135 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 139..147 FT /evidence="ECO:0007829|PDB:2BKW" FT TURN 148..151 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 156..166 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 170..175 FT /evidence="ECO:0007829|PDB:2BKW" FT TURN 177..182 FT /evidence="ECO:0007829|PDB:2BKW" FT TURN 187..191 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 216..222 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 238..249 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 261..277 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 279..294 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 295..300 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 319..322 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 326..335 FT /evidence="ECO:0007829|PDB:2BKW" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 349..351 FT /evidence="ECO:0007829|PDB:2BKW" FT STRAND 352..355 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:2BKW" FT HELIX 369..380 FT /evidence="ECO:0007829|PDB:2BKW" SQ SEQUENCE 385 AA; 41907 MW; 460D5DCCA8FDF79F CRC64; MTKSVDTLLI PGPIILSGAV QKALDVPSLG HTSPEFVSIF QRVLKNTRAV FKSAAASKSQ PFVLAGSGTL GWDIFASNFI LSKAPNKNVL VVSTGTFSDR FADCLRSYGA QVDVVRPLKI GESVPLELIT EKLSQNSYGA VTVTHVDTST AVLSDLKAIS QAIKQTSPET FFVVDAVCSI GCEEFEFDEW GVDFALTASQ KAIGAPAGLS ISLCSSRFMD YALNDSKNGH VHGYFSSLRR WTPIMENYEA GKGAYFATPP VQLINSLDVA LKEILEEGLH KRWDLHREMS DWFKDSLVNG LQLTSVSRYP SNMSAHGLTA VYVADPPDVI AFLKSHGVVI AGGIHKDIGP KYIRIGHMGV TACNKNLPYM KNCFDLIKLA LQRKK //