MASY_CANTR
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 03-AUG-2022, entry version 83.
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}.
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; 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; 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; 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