AGX1_YEAST
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 03-AUG-2022, entry version 170.
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 (2.57 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE
RP AND GLYOXYLATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, DISRUPTION 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}.
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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 PDBsum; 2BKW; -.
DR AlphaFoldDB; P43567; -.
DR SMR; P43567; -.
DR BioGRID; 31116; 38.
DR DIP; DIP-5433N; -.
DR IntAct; P43567; 3.
DR STRING; 4932.YFL030W; -.
DR MaxQB; P43567; -.
DR PaxDb; P43567; -.
DR PRIDE; P43567; -.
DR EnsemblFungi; YFL030W_mRNA; YFL030W; YFL030W.
DR GeneID; 850514; -.
DR KEGG; sce:YFL030W; -.
DR SGD; S000001864; AGX1.
DR VEuPathDB; FungiDB:YFL030W; -.
DR eggNOG; KOG2862; Eukaryota.
DR GeneTree; ENSGT00940000153241; -.
DR HOGENOM; CLU_027686_5_2_1; -.
DR InParanoid; P43567; -.
DR OMA; KNWLPIM; -.
DR BioCyc; MetaCyc:MON3O-372; -.
DR BioCyc; YEAST:MON3O-372; -.
DR BRENDA; 2.6.1.44; 984.
DR SABIO-RK; P43567; -.
DR UniPathway; UPA00288; UER00428.
DR EvolutionaryTrace; P43567; -.
DR PRO; PR:P43567; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43567; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IDA:SGD.
DR GO; GO:0004760; F:serine-pyruvate transaminase activity; IBA:GO_Central.
DR GO; GO:0019265; P:glycine biosynthetic process, by transamination of glyoxylate; IDA:SGD.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
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..298
FT /evidence="ECO:0007829|PDB:2BKW"
FT TURN 299..301
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
