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Database: UniProt
Entry: C5DTL1_ZYGRC
LinkDB: C5DTL1_ZYGRC
Original site: C5DTL1_ZYGRC 
ID   C5DTL1_ZYGRC            Unreviewed;       438 AA.
AC   C5DTL1;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN   OrderedLocusNames=ZYRO0C09416g {ECO:0000313|EMBL:CAR27122.1};
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR27122.1, ECO:0000313|Proteomes:UP000008536};
RN   [1] {ECO:0000313|Proteomes:UP000008536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229 {ECO:0000313|Proteomes:UP000008536};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(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; CU928175; CAR27122.1; -; Genomic_DNA.
DR   RefSeq; XP_002496055.1; XM_002496010.1.
DR   AlphaFoldDB; C5DTL1; -.
DR   STRING; 559307.C5DTL1; -.
DR   GeneID; 8203267; -.
DR   KEGG; zro:ZYRO0C09416g; -.
DR   HOGENOM; CLU_022158_2_2_1; -.
DR   InParanoid; C5DTL1; -.
DR   UniPathway; UPA00033; UER00028.
DR   Proteomes; UP000008536; Chromosome C.
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; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008536};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          38..291
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   438 AA;  48748 MW;  AC94C64877CF5234 CRC64;
     MSDNKEFQPV TESTAPKTRQ VNPYGPNPAD YLSNVENFQL IDSTLREGEQ FANAFFDTEK
     KIEIAKALDA FGVDYIELTS PVASEQSRRD CEAICKLGLK SKILTHIRCH MDDAKVAVET
     GVDGVDVVIG TSKFLRQYSH GKDMNYIAKS AVEVIEFVKS KGIEIRFSSE DSFRSDLVDL
     LNIYKTVSQI GVNRVGIADT VGCANPRQVY ELIRTLKSVV SCDIECHFHN DTGCAIPNAY
     CALEAGARLI DTCVLGIGER NGIVPLGGLM ARMIVAAPEY VKSKYKLHKL RDLEVLVAEA
     VEVNIPFNNP ITGFSAFTHK AGIHAKAILA NPSTYEILNP HDFGMKRYIH FANRLTGWNA
     IKTRVDQLNL NLTDQQCKDV TQKIKKLGDI RQLTVDDVDS IIKDFHAEVS TPQLQPKRDN
     DDIQDEISEE PATKKSHQ
//
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