ID C4YAG2_CLAL4 Unreviewed; 417 AA.
AC C4YAG2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN ORFNames=CLUG_05100 {ECO:0000313|EMBL:EEQ40973.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40973.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ40973.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40973.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408081; EEQ40973.1; -; Genomic_DNA.
DR RefSeq; XP_002615086.1; XM_002615040.1.
DR AlphaFoldDB; C4YAG2; -.
DR STRING; 306902.C4YAG2; -.
DR GeneID; 8495553; -.
DR KEGG; clu:CLUG_05100; -.
DR VEuPathDB; FungiDB:CLUG_05100; -.
DR HOGENOM; CLU_022158_2_2_1; -.
DR InParanoid; C4YAG2; -.
DR OMA; DWSNGMR; -.
DR OrthoDB; 2781767at2759; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000007703; 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; PS00815; AIPM_HOMOCIT_SYNTH_1; 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:UP000007703};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 19..278
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 46076 MW; 094CEE0B9C03E80A CRC64;
MSNPYGPNPH DFLSNVNKFE VIESTLREGE QFANAFFSTE KKIEIAKALD DFGVDYIELT
SPVASEQSRR DCEAICKLGL KAKILTHIRC HMDDARVAVE TGVDGVDVVI GTSQFLRQYS
HGKDMNYIAQ SAIEVIEFVK SKGIEIRFSS EDSFRSDIVD LLNIYKTVDK IGVNRVGIAD
TVGCANPRQV YDLVKTLKSV VSCDIECHFH NDTGCAIANA YTALEAGAKL IDVSVLGIGE
RNGITPLGAL MARMITADRD YVLSKYKLHK LRDLENLVAD AVQVNIPFNN PITGFCAFTH
KAGIHAKAIL ANPSTYEILN PSDFGLTRYI HFANRLTGWN AIKSRVDQLN LHLTDAQCKE
VTHKIKLLGD VRQLNIDDVD SIIKDYHYEV TTPSLAPVNG ADDVPDAEPA AKKQKSE
//
