MLS2_YEAST
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 03-AUG-2022, entry version 171.
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; 42.
DR DIP; DIP-6744N; -.
DR IntAct; P21826; 1.
DR STRING; 4932.YIR031C; -.
DR MaxQB; P21826; -.
DR PaxDb; P21826; -.
DR PRIDE; P21826; -.
DR EnsemblFungi; YIR031C_mRNA; YIR031C; YIR031C.
DR GeneID; 854849; -.
DR KEGG; sce:YIR031C; -.
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; CHKRGAP; -.
DR BioCyc; MetaCyc:YIR031C-MON; -.
DR BioCyc; YEAST:YIR031C-MON; -.
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; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR006252; Malate_synthA.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR019830; Malate_synthase_CS.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR PANTHER; PTHR42902; PTHR42902; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR PIRSF; PIRSF001363; Malate_synth; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01344; malate_syn_A; 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
