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Database: UniProt
Entry: A0A061H2H0_9BASI
LinkDB: A0A061H2H0_9BASI
Original site: A0A061H2H0_9BASI 
ID   A0A061H2H0_9BASI        Unreviewed;       532 AA.
AC   A0A061H2H0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=malate synthase {ECO:0000256|ARBA:ARBA00012636};
DE            EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636};
GN   ORFNames=PFL1_05562 {ECO:0000313|EMBL:EPQ26927.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26927.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ26927.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26927.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(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   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|ARBA:ARBA00006394}.
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DR   EMBL; KE361642; EPQ26927.1; -; Genomic_DNA.
DR   RefSeq; XP_007881289.1; XM_007883098.1.
DR   AlphaFoldDB; A0A061H2H0; -.
DR   GeneID; 19319652; -.
DR   KEGG; pfp:PFL1_05562; -.
DR   eggNOG; KOG1261; Eukaryota.
DR   HOGENOM; CLU_018928_3_0_1; -.
DR   OrthoDB; 177378at2759; -.
DR   Proteomes; UP000053664; Unassembled WGS sequence.
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   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; 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.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          4..67
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          160..404
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          410..523
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        445
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   532 AA;  59592 MW;  243B9016336B8893 CRC64;
     MSVEGVRVLG KVEGDHAEIV TPEALRFLAV LHRSFESTRQ SLLKNRQLRQ TRFDGGALPD
     FLPETAHIRN DPTWQCAPPA PGLRDRRVEI TGPVDRKMVI NALNSGAYTY MADFEDSNSP
     TWANCLDGQV NMRAAINRTI DFKQSNGKEY KLKPQGQTAT LIIRPRGWHL NEEHILVDGK
     PMSGGLVDFG LYFFHNAHTL VRNGFGPYFY LPKMESHLEA RLWNDVFNLS QDYIKMPRGT
     IRGTVLIETI TAAFEMDEIL YELRHHSSGL NCGRWDYIFS FIKRQRYSKG AILPDRSAVT
     MTVPFMQAYV NLLIQTCHKR SVAAIGGMAA QIPIKDDPKA NEAAMEKVRA DKLREVQAGH
     DGTWVAHPAL VKIALEIFDK HMLGPNQYHV RREEVKVSAL DLLNSNVPGQ ITEAGVRANV
     AALLVYCANW LNGLGCVPVA NMMEDAATGE ISRLGLWSWV YHQQKTAEGN AITPAYIDRI
     LDEEAAKVSK IGKSVDVAKR YIADQMRANA PDEFLTSALY AHLPHNHAPA RI
//
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