ID   MASY_CANTR              Reviewed;         551 AA.
AC   Q02216;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Malate synthase, glyoxysomal;
DE            EC=2.3.3.9;
GN   Name=PMS1;
GN   and
GN   Name=PMS2;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1794980; DOI=10.1093/oxfordjournals.jbchem.a123688;
RA   Hikada M., Atomi H., Fukuda Y., Aoki A., Hishida T., Teranishi Y., Ueda M.,
RA   Tanaka A.;
RT   "Presence of two transcribed malate synthase genes in an n-alkane-utilizing
RT   yeast, Candida tropicalis.";
RL   J. Biochem. 110:909-914(1991).
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   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome.
CC   -!- MISCELLANEOUS: There are two genes for malate synthase in C.tropicalis.
CC       The sequence shown is that of PMS1, PMS2 differs at a single position.
CC   -!- SIMILARITY: Belongs to the malate synthase family. {ECO:0000305}.
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DR   EMBL; D13415; BAA02680.1; -; Genomic_DNA.
DR   EMBL; D13416; BAA02681.1; -; Genomic_DNA.
DR   PIR; JX0195; JX0195.
DR   PIR; JX0196; JX0196.
DR   AlphaFoldDB; Q02216; -.
DR   SMR; Q02216; -.
DR   VEuPathDB; FungiDB:CTMYA2_005440; -.
DR   VEuPathDB; FungiDB:CTRG_03389; -.
DR   UniPathway; UPA00703; UER00720.
DR   GO; GO:0009514; C:glyoxysome; 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; 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   3: Inferred from homology;
KW   Glyoxylate bypass; Glyoxysome; Peroxisome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..551
FT                   /note="Malate synthase, glyoxysomal"
FT                   /id="PRO_0000166860"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        458
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   VARIANT         159
FT                   /note="N -> S (in PMS2)"
SQ   SEQUENCE   551 AA;  62449 MW;  A74A587A9F22C8EC CRC64;
     MSTPFPKTAD KVKGVQILGP IPDEAKHIFN QETLAFVATL HRGFEARRQE LLNNRKEQQK
     LRDQGFLPDF LPETEYIRND STWTGPALAP GLIDRRCEIT GPTDRKMVIN ALNSNVATYM
     ADFEDSLTPA WKNLVEGQVN LYDAVRRNLS ATINGKQYNL NLEKGRHIPT LIVRPRGWHL
     TEKHVLVDGT PVSGGIFDFA VYFYNSAKEA IAQGFGPYFY LPKMEHHLEA KLWNDIFNYS
     QDYIGLKRGT IRASVLIETI PAVFQMDEII YQLREHSAGL NCGRWDYIFS YIKCLRNHPD
     FILPDRSQVT MAAPFMSSYV KLLVHTTHKR KVHALGGMAA QIPIKDDEAR NRAALENVTK
     DKLREVTLGC DSCWVAHPAL VPVVLKVFNE HMKGPNQISL PPKEPFKPIT QRDLLSPFVP
     GAKITEQGIR ANIVIGISYI EAWLRNVGCV PINYLMEDAA TAEVSRTQIW QWVTHGAKTD
     TGKVITKEYV KQLLDEEYAK LTKNAKPGNK FKRAFEYFAP EALGEKYSDF VTTLIYDDVT
     TIGRALPGER L
//