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Database: UniProt
Entry: S0E5R9_GIBF5
LinkDB: S0E5R9_GIBF5
Original site: S0E5R9_GIBF5 
ID   S0E5R9_GIBF5            Unreviewed;       542 AA.
AC   S0E5R9;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Malate synthase {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
DE            EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
GN   ORFNames=FFUJ_06213 {ECO:0000313|EMBL:CCT70259.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT70259.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
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         ECO:0000256|RuleBase:RU000555};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2. {ECO:0000256|RuleBase:RU000555}.
CC   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|ARBA:ARBA00006394, ECO:0000256|RuleBase:RU000555}.
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DR   EMBL; HF679028; CCT70259.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0E5R9; -.
DR   STRING; 1279085.S0E5R9; -.
DR   EnsemblFungi; CCT70259; CCT70259; FFUJ_06213.
DR   VEuPathDB; FungiDB:FFUJ_06213; -.
DR   HOGENOM; CLU_018928_3_0_1; -.
DR   OrthoDB; 177378at2759; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000016800; Chromosome 6.
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   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW   ECO:0000256|RuleBase:RU000555};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000555};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU000555}.
FT   DOMAIN          10..72
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          164..408
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          415..530
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   542 AA;  61125 MW;  73AE3D9A77F1D786 CRC64;
     MASVDSVLQG VSVSGKVDDI HRKILTPEAL AFLALLHRSF NERRKNLLER RKARQAELDR
     GVLPDFLPET KHIRENPTWK GAPPAPGLVD RRVEITGPTD RKMVVNALNA NVYTYMADFE
     DSSAPTWDNM INGQVNLYDA NRRQVDFKQG QKEYKLRTDR KLPTLIVRPR GWHLEEKHVT
     VDGEPISGSL FDFGLYFFHN AFETQRQGFG PYFYLPKMES HLEARLWNDA FNLAQDYIGM
     PRGTIRGTVL IETILAAFEM DEIIYELRDH SSGLNCGRWD YIFSVIKKFR NNPNFVLPDR
     SAVTMTVPFM ESYVKLLIQT CHKRGVHAMG GMAAQIPIKN DTAANDKAME GVRADKLREV
     RAGHDGTWVA HPALASIATE IFDKHMPTPN QLFVRREDVT IGQNDLLNMN VPGTVTEEGI
     KKNLNIGLGY MEAWIRGVGC VPINYLMEDA ATAEVSRSQL WQWVKHGVNT AEGKRVDKSY
     ALKLLKEVAD QLAASAPKGN KYHLAAQYFS SQVTGEDYAD FLTTLLYNEI TQAGPPSPAS
     KL
//
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