ID A0A085MDE1_9BILA Unreviewed; 897 AA.
AC A0A085MDE1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN ORFNames=M513_03878 {ECO:0000313|EMBL:KFD55237.1}, M514_03878
GN {ECO:0000313|EMBL:KFD65963.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD55237.1, ECO:0000313|Proteomes:UP000030764};
RN [1] {ECO:0000313|EMBL:KFD55237.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD65963.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD55237.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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:0000256|ARBA:ARBA00001699};
CC -!- SIMILARITY: Belongs to the malate synthase family.
CC {ECO:0000256|ARBA:ARBA00006394}.
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DR EMBL; KL363201; KFD55237.1; -; Genomic_DNA.
DR EMBL; KL367530; KFD65963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085MDE1; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; Unassembled WGS sequence.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
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 Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR006252; Malate_synthA.
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 InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01344; malate_syn_A; 1.
DR PANTHER; PTHR42902; MALATE SYNTHASE; 1.
DR PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1.
DR Pfam; PF00463; ICL; 1.
DR Pfam; PF20659; MS_C; 1.
DR Pfam; PF20656; MS_N; 1.
DR Pfam; PF01274; MS_TIM-barrel; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51645; Malate synthase G; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 387..434
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 527..760
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 777..892
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 531
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 811
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
SQ SEQUENCE 897 AA; 101048 MW; B21338B322030C0A CRC64;
MARAGLKSIY LSGWQVAADN NSAGMMYPDQ SLYPANSGPE LCQRLNRTLL RADQIEHIEA
NVTRDWLLPI VADAEAGFGG PLNCYEIMRA YIEAGAAGVH YEDQLASEKK CGHLGGKVLI
PTSSHIRNLT AARLAADVCG VPVVIICRTD AESARLITND VDERDRPFID TTVGRTTEGF
FHLKEDTGLQ HCISRSIAYA PYADLLWMET SKPNLQEAIL FAEAVRRVYP DKLLAYNCSP
SFNWSANLDR QTIRTFQSEL AKMGYKYQFV TLAGFHCINY SMFKLAKYYQ TYGMEAYSNL
QQNEMQSEEE GYTAVHHQRE VGVQYYDCIS QVITLGQSST VGLVDSTETD QFVLHRTTQA
RGIHSAQAVG FRNNGKLALT LPPVDDVILS DAAMDFLVEL HEKFEPERRK LLDRRVERQA
ALNAGQLPNF LADTSDIRMG EWAVAKAPND LQDRRVEITG PLDRKMVINA FNSGAKAFMA
DFEDSTSPTW QNVVSGQRNL YDAVRGQIDY EDPNTTKKYC LTERPAVLMV RPRGWHLDER
HVGIGGQPMS ASLFDFGLFA FHNASALEAK GSGAYYYLPK MESHLEAKLW KQVFDFTKDR
LGLKVGTLRS TALVEHMLAT FEIEEILHSM KEYMVGLNCG RWDYIFSYIK AFRHHPNYLL
PDREQVTMTV PFMRAYAKYV IKICHKRGAH AIGGMSAFIP VKSDPELNQR AFSQVRQDKE
REANDGHDGT WVAHPGLVPV AMDIFNKAMP QPNQLDKQLV DFAPQPADFV AVPAGSRTEE
GLRRNVSVTL GYMEAWLRGN GCVPLYNLME DAATAEISRS QLWQWVRHNG KLADGRSITW
SFVDKVISEE VEEWKRRGVK SATLIEAADL LKELTVSKEM PEFLTLKAYD KLIKKGL
//
