ID   MASY_CUCMA              Reviewed;         566 AA.
AC   P24571;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=Malate synthase, glyoxysomal;
DE            EC=2.3.3.9;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 83-91; 197-206 AND
RP   417-426.
RC   STRAIN=cv. Kurokawa Amakuri Nankin; TISSUE=Etiolated cotyledon;
RX   PubMed=1709098; DOI=10.1111/j.1432-1033.1991.tb15915.x;
RA   Mori H., Takeda-Yoshikawa Y., Hara-Nishimura I., Nishimura M.;
RT   "Pumpkin malate synthase. Cloning and sequencing of the cDNA and northern
RT   blot analysis.";
RL   Eur. J. Biochem. 197:331-336(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   -!- SIMILARITY: Belongs to the malate synthase family. {ECO:0000305}.
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DR   EMBL; X56948; CAA40262.1; -; mRNA.
DR   AlphaFoldDB; P24571; -.
DR   SMR; P24571; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000504608; Unplaced.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glyoxylate bypass; Glyoxysome; Peroxisome;
KW   Reference proteome; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..566
FT                   /note="Malate synthase, glyoxysomal"
FT                   /id="PRO_0000166867"
FT   MOTIF           564..566
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        467
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   566 AA;  64636 MW;  B77F77D1D593834A CRC64;
     MGSLGMYSES AVRKKSSRGY DVPEGVDIRG RYDEEFARIL NKEALLFVAD LQRTFRNHIR
     YSMECRREAK RRYNEGAVPG FDPATKYIRE SEWTCASVPP AVADRRVEIT GPVERKMIIN
     ALNSGAKVFM ADFEDALSPN WENLMRGQIN LKDAVDGTIS FHDKARNKVY KLNDQTAKLF
     VRPRGWHFAE AHIFIDGEPA TGCLVDFGLY FFHNHANFRR SQGQGSGPFF YLPKMEHSRE
     AKIWNSVFER AEKMAGIERG SIRATVLIET LPAVFQMDEI LYELRDHSVG LNCGRWDYIF
     SYVKTFQAHL DRLLPDRVQV GMAQHFMRSY SDLLIRTCHT VVCHVGGMAA QIPIRDDPKA
     NEMALELVRK DKLREAKAGH DGTWAAHPGL IPACMEVFTN SMGNAPNQIR SARRDDAANL
     TEDDLLQQPR GVRTLEGLRL NTRVGIQYLA AWLTGTGSVP LYNLMEDAAT AEISRVQNWQ
     WLKYGVELDG DGLGVRVNKE LFARVVEEEM ERIEREVGKE KFRKGMYKEA CKMFTRQCTA
     PTLDDFLTLD AYNHIVIHHP RELSRL
//