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MASY_CUCSA
ID   MASY_CUCSA              Reviewed;         568 AA.
AC   P08216;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Malate synthase, glyoxysomal;
DE            EC=2.3.3.9;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Long green ridge;
RX   PubMed=2491683; DOI=10.1007/bf00016022;
RA   Graham I.A., Smith L.M., Brown J.W.S., Leaver C.J., Smith S.M.;
RT   "The malate synthase gene of cucumber.";
RL   Plant Mol. Biol. 13:673-684(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 475-568.
RX   PubMed=16664899; DOI=10.1104/pp.81.3.762;
RA   Smith S.M., Leaver C.J.;
RT   "Glyoxysomal malate synthase of cucumber: molecular cloning of a cDNA and
RT   regulation of enzyme synthesis during germination.";
RL   Plant Physiol. 81:762-767(1986).
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; X15425; CAA33465.1; -; Genomic_DNA.
DR   EMBL; M16219; AAA33123.1; -; mRNA.
DR   PIR; S07550; SYKVMA.
DR   AlphaFoldDB; P08216; -.
DR   SMR; P08216; -.
DR   STRING; 3659.XP_004152519.1; -.
DR   eggNOG; KOG1261; Eukaryota.
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   2: Evidence at transcript level;
KW   Glyoxylate bypass; Glyoxysome; Peroxisome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..568
FT                   /note="Malate synthase, glyoxysomal"
FT                   /id="PRO_0000166868"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           566..568
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        469
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        475
FT                   /note="I -> G (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   568 AA;  64961 MW;  0C25AB66288ECAA4 CRC64;
     MGSLGMYSES GLTKKGSSRG YDVPEGVDIR GRYDEEFAKI LNKEALLFIA DLQRTFRNHI
     KYSMECRREA KRRYNEGGLP GFDPATKYIR DSEWTCAPVP PAVADRRVEI TGPVERKMII
     NALNSGAKVF MADFEDALSP NWENLMRGQI NLKDAVDGTI SFHDRVRNRV YKLNDRTAKL
     FVRPRGWHLP EAHIFIDGEP ATGCLVDFGL YFFHNHANFR RSQGQGYGPF FYLPKMEHSR
     EAKIWNSVFE RAEKMAGIER GSIRATVLIE TLPAVFQMNE ILYELRDHSV GLNCGRWDYI
     FSYVKTFQAH PDRLLPDRVL VGMTQHFMRS YSDLLIRTCH RRGVHAMGGM AAQIPIRDDP
     KANEVALELV RKDKLREVKA GHDGTWAAHP GLIPACMEVF TNNMGNAPNQ IRSMRRDDAA
     NLTEEDLLQQ PRGVRTMEGL RLNTRVGIQY LAAWLTGAGS VPLYNLAEDA ATAEISRVQN
     WQWLKYGVEL DGDGLGVRVN KELFGRVVEE EMERIEREVG KERFKKGMYK EACKMFTRQC
     TAPNLDDFLT LDAYNYIVIH HPRELSKL
 
 
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