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Database: UniProt
Entry: A0A2B7Z5Y0_9EURO
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ID   A0A2B7Z5Y0_9EURO        Unreviewed;       539 AA.
AC   A0A2B7Z5Y0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=GX50_08630 {ECO:0000313|EMBL:PGH28623.1};
OS   Emmonsia crescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH28623.1, ECO:0000313|Proteomes:UP000226031};
RN   [1] {ECO:0000313|EMBL:PGH28623.1, ECO:0000313|Proteomes:UP000226031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH28623.1,
RC   ECO:0000313|Proteomes:UP000226031};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-2017) 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         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}.
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:PGH28623.1}.
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DR   EMBL; PDND01000360; PGH28623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7Z5Y0; -.
DR   STRING; 73230.A0A2B7Z5Y0; -.
DR   VEuPathDB; FungiDB:EMCG_03203; -.
DR   OrthoDB; 177378at2759; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000226031; Unassembled WGS sequence.
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:UP000226031};
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          9..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   539 AA;  60699 MW;  E331BEAB7A4CFB92 CRC64;
     MATVETLLKG VAILGPLNDQ TRKILTKDAT AFVALLHRTF NPTRKALLQR RIDRQAEIDR
     GTLLDFLPET KHIRENDAWK GAPPAPGLVD RRVEITGPTD RKMVVNALNS DVYTYMADFE
     DSTAPTWENM VNGQVNLYDA IRRQVDFKQG GKEYKLRTDR KLPTLITRAR GWHLDEKHMT
     VDGEPVSGSL FDFGLYFFHN GKELVNRGAG PYFYLPKLES HLEARLWNDV FNLAQDYIGM
     PRGTIRGTVL IETITAAFEM DEIIYELKEH SSGLNCGRWD YIFSFIKKFR QNPNFVLPDR
     SAVTMTVPFM DAYVKLLIKT CHRRGVHAMG GMAAQIPIKD DPKANDAAMA SVRADKLREA
     RAGHDGTWVA HPALAKIATD IFDQYMPTPN QLFVRREDVH ITANDLLNTN VPGSVTEDGI
     RKNLNIGLSY MEGWLRGVGC IPINYLMEDA ATAEVSRSQL WQWVRHNITT AEGKRVDKGY
     ALKLLQEQAD QLATNGPKGN KYQLAARYFA SQVTGEDYAD FLTSLLYNEI SAPGSAAKL
//
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