ID A0A2H9TPU9_9FUNG Unreviewed; 1125 AA.
AC A0A2H9TPU9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN ORFNames=PSACC_00432 {ECO:0000313|EMBL:PJF19788.1};
OS Paramicrosporidium saccamoebae.
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Paramicrosporidium.
OX NCBI_TaxID=1246581 {ECO:0000313|EMBL:PJF19788.1, ECO:0000313|Proteomes:UP000240830};
RN [1] {ECO:0000313|EMBL:PJF19788.1, ECO:0000313|Proteomes:UP000240830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSL3 {ECO:0000313|EMBL:PJF19788.1,
RC ECO:0000313|Proteomes:UP000240830};
RA Quandt C.A., Beaudet D., Corsaro D., Michel R., Corradi N., James T.;
RT "The genome of Paramicrosporidium saccamoebae is the missing link in
RT understanding Cryptomycota and Microsporidia evolution.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PJF19788.1}.
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DR EMBL; MTSL01000041; PJF19788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9TPU9; -.
DR STRING; 1246581.A0A2H9TPU9; -.
DR Proteomes; UP000240830; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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; cd00727; malate_synt_A; 1.
DR CDD; cd00174; SH3; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 3.20.20.360; Malate synthase, domain 3; 1.
DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR010422; Ccdc124/Oxs1.
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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR NCBIfam; TIGR01344; malate_syn_A; 1.
DR PANTHER; PTHR42902; MALATE SYNTHASE; 1.
DR PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1.
DR Pfam; PF03114; BAR; 2.
DR Pfam; PF06244; Ccdc124; 1.
DR Pfam; PF20659; MS_C; 1.
DR Pfam; PF20656; MS_N; 1.
DR Pfam; PF01274; MS_TIM-barrel; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF51645; Malate synthase G; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00510; MALATE_SYNTHASE; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW Reference proteome {ECO:0000313|Proteomes:UP000240830};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 784..843
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 741..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..694
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 759..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 446
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601465-50"
SQ SEQUENCE 1125 AA; 127211 MW; A82C6867DCA05A43 CRC64;
MVNASGFTLL GKPKPEYSTI LGPESQAFLV VLHRCFEGRR QQLLEKRRQR QAELDLGILP
DFLPETEFVR KDDTWKAAPP ALGLIDRRVE ITGPVDRKMV INALNSKATQ FMADFEDSTS
PTWENVMSGQ VNLRDANKRS IRFEAPNGKR YELNDGGNLP TLLVRPRGWH LEECHVLIDG
KPMSASLFDF GLYFFHNAHQ TLKIGQGPYF YLPKMESHLE ARLWNDVFNL SQDYLNLPRG
TIRATVLIET ILAAFEMDEI IYELREHSAG LNCGRWDYIF SFIKKFHKHP KFVLPDRSAV
TMSVPFMKAY VELLIKTCHK RGVHAMGGMA AQIPIKNNPE LNRAAMEKVK EDKTREVLAG
HDGTWVAHPD LIPLAKDIFD AHMPQPNQLF VRRDEICVLS EQLIDPGVEV SITKQGVTEN
TRAALVYISS WLKGNGCVPI NNLMEDAATA EIARAQLWQW IHHNCITIDT REAITVPWVQ
RIILDEVGND PSKSLAADKL LHMLENDKFE DFLTSLCYPD ITVVERPSKV SPYAWTGEKL
GTAEKTNVSE DFRRLDLETE SRKDGIEKLT ISLTDYAKTL DKRSSQDKKV SAMSMLSKAM
IQQGKFHGES TMIGLALAEI VRKGLLMESM ALYTSMKDYD SMKKKLENRR LDYDAKLNKF
NKSKKDKPGL EEEMKTAQKK YNETLADIES LMSTFAEREV LAIKSSMQSK LDSNAATVDK
AILIRKNSNI KTVLPAGLET QTTKSEIGNS HGEQELRSET PKPISNVSGN ATTRVTRNAS
VNRPEKEIVE ALYDFTAENE GELSISKGDK INVTEHIDEG WWYGENDGYK GIFPANYVRR
ISSVAHEAEG RKSMRSTSNG SVTSNRKPVV QASSRRPIVP DWPTMGKGFA VNSKAQEGRE
RKAAHKEMKT REEEKKQEEK VSKEWQVGAK TKSSKQVSEE QKRHDKAQRK LERERLEAQE
ATELGKLKPV HPLPKEKKAS PVVKTAMSIQ SSASSVTSVQ TNTSHTELLS ETAPEYSASN
IDDALFLLDA TSSNLTKSGV ERHPERRMKA AYASFEEREM PLLKEQFPGL RLSQLKEKLY
KLWQKSPDNP FNQTHISYNS TRSQEVLKTT SEIEANLDRL KLPPA
//
