ID G3B8G8_CANTC Unreviewed; 324 AA.
AC G3B8G8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN ORFNames=CANTEDRAFT_115851 {ECO:0000313|EMBL:EGV62893.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV62893.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996527; EGV62893.1; -; Genomic_DNA.
DR RefSeq; XP_006689063.1; XM_006689000.1.
DR AlphaFoldDB; G3B8G8; -.
DR GeneID; 18248055; -.
DR KEGG; cten:CANTEDRAFT_115851; -.
DR HOGENOM; CLU_022158_2_0_1; -.
DR OrthoDB; 2781767at2759; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000000707; 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 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:UP000000707};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..187
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 303..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 35669 MW; 9795399D71AA552C CRC64;
MDDAKVAVET GVDGVDVVIG TSSFLRQYSH GKDMNYIAQS AVEVIEFVKS KGIEIRFSSE
DSFRSDLVDL LNIYRTVDKI GVNRVGIADT VGCANPRQVY ELVRTLKSVV NCDIECHFHN
DTGCAIANAY TALEGGAKLI DVSVLGIGER NGITPLGGLM ARMIAADRDY VLSKYKLHKL
RDLENLVAEA VQVNIPFNNP ITGFCAFTHK AGIHAKAILA NPSTYEILNP SDFGLTRYIH
FANRLTGWNA IKARVDQLNL HLSDEQCKEV TNKIKKLGDV RQLNIDDVDS IIKDFHADIS
TPLIKPSADG QEPDELPIKK AKLQ
//
