ID   MLS2_YEAST              Reviewed;         554 AA.
AC   P21826; D6VVW2;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Malate synthase 2 {ECO:0000303|PubMed:8462696};
DE            EC=2.3.3.9 {ECO:0000250|UniProtKB:Q9LZC3};
DE   AltName: Full=Degradation of allantoin protein 7 {ECO:0000303|PubMed:3915539};
GN   Name=DAL7 {ECO:0000303|PubMed:3915539};
GN   Synonyms=MLS2 {ECO:0000303|PubMed:8462696}; OrderedLocusNames=YIR031C;
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 [GENOMIC DNA].
RC   STRAIN=RH218;
RX   PubMed=2552287; DOI=10.1128/mcb.9.8.3231-3243.1989;
RA   Yoo H.S., Cooper T.G.;
RT   "The DAL7 promoter consists of multiple elements that cooperatively mediate
RT   regulation of the gene's expression.";
RL   Mol. Cell. Biol. 9:3231-3243(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=8462696; DOI=10.1016/0014-5793(93)80601-p;
RA   Fernandez E., Fernandez M., Rodicio R.;
RT   "Two structural genes are encoding malate synthase isoenzymes in
RT   Saccharomyces cerevisiae.";
RL   FEBS Lett. 320:271-275(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [4]
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   [5]
RP   IDENTIFICATION, AND INDUCTION.
RX   PubMed=3915539; DOI=10.1128/mcb.5.9.2279-2288.1985;
RA   Yoo H.S., Genbauffe F.S., Cooper T.G.;
RT   "Identification of the ureidoglycolate hydrolase gene in the DAL gene
RT   cluster of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 5:2279-2288(1985).
RN   [6]
RP   INTERACTION WITH PEX9, AND SUBCELLULAR LOCATION.
RX   PubMed=27678487; DOI=10.1242/jcs.195271;
RA   Effelsberg D., Cruz-Zaragoza L.D., Schliebs W., Erdmann R.;
RT   "Pex9p is a new yeast peroxisomal import receptor for PTS1-containing
RT   proteins.";
RL   J. Cell Sci. 129:4057-4066(2016).
CC   -!- FUNCTION: Allantoin metabolism-specific malate synthase involved in the
CC       recycling the glyoxylate generated during allantoin degradation by the
CC       ureidoglycollate (UG) hydrolase reaction. {ECO:0000269|PubMed:8462696}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC         Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.3.9;
CC         Evidence={ECO:0000250|UniProtKB:Q9LZC3};
CC   -!- SUBUNIT: Interacts with PEX9. {ECO:0000269|PubMed:27678487}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:27678487}.
CC       Note=Imported in peroxisome via recognition by the peroxisomal
CC       targeting signal receptor PEX9. {ECO:0000269|PubMed:27678487}.
CC   -!- INDUCTION: Expression is insensitive to carbon catabolite repression,
CC       but highly sensitive to nitrogen catabolite repression
CC       (PubMed:8462696). Its expression is induced by allophanate or oxalurate
CC       (PubMed:3915539). {ECO:0000269|PubMed:3915539,
CC       ECO:0000269|PubMed:8462696}.
CC   -!- DISRUPTION PHENOTYPE: Diminishes the ureidoglycollate hydrolase
CC       activity by 3 to 4 fold. {ECO:0000269|PubMed:2552287}.
CC   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000269|PubMed:3915539}.
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DR   EMBL; M28124; AAA50351.1; -; Genomic_DNA.
DR   EMBL; Z38061; CAA86191.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08578.1; -; Genomic_DNA.
DR   PIR; S48493; S48493.
DR   RefSeq; NP_012297.3; NM_001179553.3.
DR   AlphaFoldDB; P21826; -.
DR   SMR; P21826; -.
DR   BioGRID; 35022; 43.
DR   DIP; DIP-6744N; -.
DR   IntAct; P21826; 1.
DR   STRING; 4932.YIR031C; -.
DR   MaxQB; P21826; -.
DR   PaxDb; 4932-YIR031C; -.
DR   PeptideAtlas; P21826; -.
DR   EnsemblFungi; YIR031C_mRNA; YIR031C; YIR031C.
DR   GeneID; 854849; -.
DR   KEGG; sce:YIR031C; -.
DR   AGR; SGD:S000001470; -.
DR   SGD; S000001470; DAL7.
DR   VEuPathDB; FungiDB:YIR031C; -.
DR   eggNOG; KOG1261; Eukaryota.
DR   GeneTree; ENSGT00940000174673; -.
DR   HOGENOM; CLU_018928_3_0_1; -.
DR   InParanoid; P21826; -.
DR   OMA; WHLPERH; -.
DR   OrthoDB; 177378at2759; -.
DR   BioCyc; MetaCyc:YIR031C-MONOMER; -.
DR   BioCyc; YEAST:YIR031C-MONOMER; -.
DR   BioGRID-ORCS; 854849; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P21826; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P21826; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0004474; F:malate synthase activity; IDA:SGD.
DR   GO; GO:0000256; P:allantoin catabolic process; IDA:SGD.
DR   GO; GO:0006097; P:glyoxylate cycle; IBA:GO_Central.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00727; malate_synt_A; 1.
DR   Gene3D; 3.20.20.360; Malate synthase, domain 3; 1.
DR   Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
DR   InterPro; IPR044856; Malate_synth_C_sf.
DR   InterPro; IPR011076; Malate_synth_sf.
DR   InterPro; IPR006252; Malate_synthA.
DR   InterPro; IPR019830; Malate_synthase_CS.
DR   InterPro; IPR001465; Malate_synthase_TIM.
DR   InterPro; IPR048355; MS_C.
DR   InterPro; IPR048356; MS_N.
DR   InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR   NCBIfam; TIGR01344; malate_syn_A; 1.
DR   PANTHER; PTHR42902; MALATE SYNTHASE; 1.
DR   PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1.
DR   Pfam; PF20659; MS_C; 1.
DR   Pfam; PF20656; MS_N; 1.
DR   Pfam; PF01274; MS_TIM-barrel; 1.
DR   PIRSF; PIRSF001363; Malate_synth; 1.
DR   SUPFAM; SSF51645; Malate synthase G; 1.
DR   PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Glyoxylate bypass; Peroxisome; Purine metabolism; Reference proteome;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..554
FT                   /note="Malate synthase 2"
FT                   /id="PRO_0000166865"
FT   MOTIF           552..554
FT                   /note="SKL peroxisome targeting motif"
FT                   /evidence="ECO:0000305|PubMed:27678487"
FT   ACT_SITE        177
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LZC3"
FT   ACT_SITE        457
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LZC3"
FT   CONFLICT        115
FT                   /note="A -> D (in Ref. 1; AAA50351 and 2; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="D -> G (in Ref. 1; AAA50351 and 2; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="P -> N (in Ref. 1; AAA50351 and 2; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  62794 MW;  006BB05371CA96CE CRC64;
     MVKISLDNTA LYADIDTTPQ FEPSKTTVAD ILTKDALEFI VLLHRTFNST RKQLLANRSN
     LQSKLDSGEY RFDFLPETEQ IRNDPTWQGA IPAPGLINRS SEITGPPLRN MLVNALNAEV
     TTYMTDFEDS SSPTWENMIY GQVNLYDAIR NQIDFKTPRK EYRLKDDISR LPTLIVRPRG
     WHMVEKHLYI DDEPISASIF DFGLYFYHNA KELVKIGKGP YFYLPKMEHH MEVKLWNDIF
     CVAQDFIGMP RGTIRATVLI ETLPAAFQME EIIYQIREHS SGLNCGRWDY IFSTIKKLRN
     LPEHVLPNRD LVTMTSPFMD AYVKRLINTC HRRGVHAMGG MAAQIPIKDD PKANEAAMNK
     VRNDKIREMK NGHDGSWVAH PALAPICNEV FSNMGTANQI YFVPDVHVTS SDLLNTKIQD
     AQVTTEGIRV NLDIGLQYME AWLRGSGCVP INHLMEDAAT AEVSRCQLYQ WVKHGVVLSD
     TGDKVTPELT AKILNEETAK LASASPLGEK NKFALAAKYF LPEVTGKIFS DFLTTLLYDE
     IIKPSAKPVD LSKL
//