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Database: UniProt
Entry: M7SWH2_EUTLA
LinkDB: M7SWH2_EUTLA
Original site: M7SWH2_EUTLA 
ID   M7SWH2_EUTLA            Unreviewed;       457 AA.
AC   M7SWH2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN   ORFNames=UCREL1_11150 {ECO:0000313|EMBL:EMR61921.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR61921.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC         H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58884; EC=2.3.3.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000523};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC         Evidence={ECO:0000256|ARBA:ARBA00000523};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC       {ECO:0000256|ARBA:ARBA00004755}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. Homocitrate synthase LYS20/LYS21 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006361}.
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DR   EMBL; KB707519; EMR61921.1; -; Genomic_DNA.
DR   RefSeq; XP_007798983.1; XM_007800792.1.
DR   AlphaFoldDB; M7SWH2; -.
DR   STRING; 1287681.M7SWH2; -.
DR   KEGG; ela:UCREL1_11150; -.
DR   eggNOG; KOG2367; Eukaryota.
DR   HOGENOM; CLU_022158_2_2_1; -.
DR   OMA; NTMRMLV; -.
DR   OrthoDB; 2781767at2759; -.
DR   UniPathway; UPA00033; UER00028.
DR   Proteomes; UP000012174; Unassembled WGS sequence.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd07948; DRE_TIM_HCS; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_02222; Homocitr_synth_fung_arch; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR048253; DRE_TIM_HCS_fun_bact.
DR   InterPro; IPR011872; Homocitrate_synth.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR02146; LysS_fung_arch; 1.
DR   PANTHER; PTHR10277:SF48; HOMOCITRATE SYNTHASE, CYTOSOLIC ISOZYME-RELATED; 1.
DR   PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          42..332
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          71..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  49949 MW;  73E4D7BDB79D3317 CRC64;
     MAAVTENTNG LNGTNGTNGT RPSQSSNPYQ PVPDFLSNVG RFKIIESTLR EGEQFANAFF
     DTGKFQSPLY NVKSTKSNRP SRNKNQDVLP LHSPPASVEY SLLYSARMLD DFGVDYIELT
     SPAASEQSRA DCEAICKLGL KAKILTHVRC HMEDAKLAVK TGVDGLDLVI GTSSLLREFS
     HGKDMTQITA SAIEVINYVK SQGLEVRFSS EDSFRSNLVD LLSLYRAVND VGVDRVGVAD
     TVGCASPRQV YDLIRTLRGV VKCDIETHFH NDTGCAIANA YVALEAGATH VDTSVIGIGE
     RNGITPLGGL MARMIVGSHD YVTGKYKLSK LKEIEDFVAE AVNINVPFNN PVTGVCAFTH
     KAGIHAKAIL ANPSTYEIIN PADFGMSRYV HFTSRLTGWN AIKSRVEQLG LKMTDEQVKL
     LTSKIKAMAD IRPLAIDDTD SIIRSFHLEH ERLEEAS
//
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