ID A0A090L3M6_STRRB Unreviewed; 967 AA.
AC A0A090L3M6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN ORFNames=SRAE_1000257200 {ECO:0000313|EMBL:CEF64317.1,
GN ECO:0000313|WBParaSite:SRAE_1000257200.1,
GN ECO:0000313|WormBase:SRAE_1000257200};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF64317.1};
RN [1] {ECO:0000313|EMBL:CEF64317.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000257200.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF64317.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000257200.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; LN609528; CEF64317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090L3M6; -.
DR STRING; 34506.A0A090L3M6; -.
DR EnsemblMetazoa; SRAE_1000257200.1; SRAE_1000257200.1; WBGene00259187.
DR WBParaSite; SRAE_1000257200.1; SRAE_1000257200.1; WBGene00259187.
DR WormBase; SRAE_1000257200; SRP06464; WBGene00259187; -.
DR eggNOG; KOG1260; Eukaryota.
DR eggNOG; KOG1261; Eukaryota.
DR OMA; IWMETSH; -.
DR OrthoDB; 177378at2759; -.
DR Proteomes; UP000035682; Chromosome X.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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; TIGR01346; isocit_lyase; 1.
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 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 Kinase {ECO:0000313|EMBL:CEF64317.1}; Lyase {ECO:0000313|EMBL:CEF64317.1};
KW Pyruvate {ECO:0000313|EMBL:CEF64317.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 452..495
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 598..827
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 846..962
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 601
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 880
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
SQ SEQUENCE 967 AA; 109077 MW; 3B46F06595E5971C CRC64;
MSQLKASNFY HIVKNSPKGR WQGIKRNYDV KDVLKLRGSV NIEYTIANKT SNKLWHLIHT
EPYVAALGAQ TGNQAVQMIK AGLKAIYLSG WQVAADGNSA GEMYPDQSLY PSNSGPELAK
RINKSLRRAD QIECAEADDM KPYRDYYAPI VADCEAGFGG SLNCFEITKA YIESGVAGVH
FEDQLGSEKK CGHMGGKVLI PISEHIRHLN AARLAADVCD TPTIIVARTD AESARLLTSD
VDERDHPFID RKAGRTSEGF YRLKDSTSME ACIQRGIAYA PYCDMIWMET SYPSLSQAKE
FAEGVKKEFP DKLFAYNCSP SFNWSKHLKK SDMEKYQREL GAMGFKYQFI TLAGFHTNSF
SIFDLAKNYR ERGMAAYAEL QKAEFDAEKS GYTAVKHQRE VGTGYFDVLA NACAGGSSST
TALTGSTEEA QFKTSTVEDD EVMTLTSEML SNDEKILTPD ALRFLRDLHN NFDRRRLSLL
ENRKIIQDKI NNDELILCFP KETEDIRRDE SWSGATIPHD MLNRKVEITG PTDRKMVINA
LNSGAKVFMA DFEDSNTPTW RNQMDGQFNL YEAVRGTIAL SHPLTGKSYK LDEKHAVLNV
RPRGLHLHEK HVLIHNKPIS GSLFDFGLFI FNNAKELIDK NSGPYFYLPK LQNADEAKWW
ADVFSYTEDK LNLPKGTIKC TVLIEHLLAS FEMEEIMYNL KDYIIGLNCG RWDYIFSYIK
VFRNHSKYLL PDRFQITMTT PFLAAYSEQV IRTCHKRKIH AMGGMAAYIP IKNNPDANNT
AITAVFNDKH REATNGHDGT WVAHPGLVDI ARDVFDQIIV GDNQIDRLLP RYASPNDLIA
IPKGTITSAG LKRNISVVLQ YLEAWLRGIG CVPLYNMMED AATAEISRAQ LWQWVKHGAK
IENGKHITPE MIQNVIATEM EPLLIRSGST SNRISEAAEM LEKFVLEPEL SEFLTNDAYD
KLVSEGR
//
