MLS1_YEAS7
ID MLS1_YEAS7 Reviewed; 554 AA.
AC A6ZRW6; B0KZS7;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Malate synthase 1 {ECO:0000250|UniProtKB:P30952};
DE EC=2.3.3.9 {ECO:0000250|UniProtKB:Q9LZC3};
GN Name=MLS1 {ECO:0000250|UniProtKB:P30952}; ORFNames=SCY_4677;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: Malate synthase which takes part in the glyoxylate cycle (By
CC similarity). MLS1 activity is essential for cells to grow on oleic acid
CC as a sole carbon source (By similarity). Two steps of the glyoxylate
CC cycle take place in the cytosol, the splitting of isocitrate into
CC succinate and glyoxylate, and the dehydrogenation of malate to
CC oxaloacetate (By similarity). However, the formation of malate from
CC glyoxylate and acetyl-CoA undertaken MLS1, occurs in the peroxisomes
CC when cells are grown on oleic acid (By similarity). The source of
CC acetyl-CoA being either peroxisomal when breaking down fatty acids, or
CC cytosolic when extra-cellular two-carbon substrates are used,
CC therefore, although not strictly essential, the peroxisomal
CC localization of MLS1 appears to be advantageous for cells growing on
CC oleic acid, in that acetyl-CoA production and utilization are thereby
CC intimately compartmentalized together to increase efficiency (By
CC similarity). {ECO:0000250|UniProtKB:P30952}.
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 -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000250|UniProtKB:Q9LZC3}.
CC -!- SUBUNIT: Interacts with PEX9. {ECO:0000250|UniProtKB:P30952}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P30952}.
CC Note=Imported in peroxisome via recognition by the peroxisomal
CC targeting signal receptor PEX9 in an oleate-dependent manner.
CC {ECO:0000250|UniProtKB:P30952}.
CC -!- SIMILARITY: Belongs to the malate synthase 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; EF125227; ABN58639.1; -; Genomic_DNA.
DR EMBL; AAFW02000067; EDN62698.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRW6; -.
DR SMR; A6ZRW6; -.
DR EnsemblFungi; EDN62698; EDN62698; SCY_4677.
DR HOGENOM; CLU_018928_3_0_1; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Glyoxylate bypass; Peroxisome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..554
FT /note="Malate synthase 1"
FT /id="PRO_0000378321"
FT MOTIF 552..554
FT /note="SKL peroxisome targeting motif"
FT /evidence="ECO:0000250|UniProtKB:P30952"
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"
SQ SEQUENCE 554 AA; 62792 MW; 6C0698E86D0F1FED CRC64;
MVKVSLDNVK LLVDVDKEPF FKPSSTTVGD ILTKDALEFI VLLHRTFNNK RKQLLENRQV
VQKKLDSGSY HLDFLPETAN IRNDPTWQGP ILAPGLINRS TEITGPPLRN MLINALNAPV
NTYMTDFEDS ASPTWNNMVY GQVNLYDAIR NQIDFDTPRK SYKLNGNVAN LPTIIVRPRG
WHMVEKHLYV DDEPISASIF DFGLYFYHNA KELIKLGKGP YFYLPKMEHH LEAKLWNDVF
CVAQDYIGIP RGTIRATVLI ETLPAAFQME EIIYQLRQHS SGLNCGRWDY IFSTIKRLRN
DPNHILPNRD QVTMTSPFMD AYVKRLINTC HRRGVHAMGG MAAQIPIKDD PAANEKAMTK
VRNDKIRELT NGHDGSWVAH PALAPICNEV FINMGTPNQI YFIPENVVTA ANLLETKIPN
GEITTEGIVQ NLDIGLQYME AWLRGSGCVP INNLMEDAAT AEVSRCQLYQ WVKHGVTLKD
TGEKVTPELT EKILKEQVER LSKASPLGDK NKFALAAKYF LPEIRGEKFS EFLTTLLYDE
IVSTKATPTD LSKL
