HOSM_YARLI
ID HOSM_YARLI Reviewed; 446 AA.
AC Q12726;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Homocitrate synthase, mitochondrial;
DE Short=HCS;
DE EC=2.3.3.14 {ECO:0000250|UniProtKB:O87198};
DE Flags: Precursor;
GN Name=LYS1; OrderedLocusNames=YALI0F31075g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=8948100;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1459::aid-yea26>3.0.co;2-m;
RA Perez-Campo F., Nicaud J.-M., Gaillardin C., Dominguez A.;
RT "Cloning and sequencing of the LYS1 gene encoding homocitrate synthase in
RT the yeast Yarrowia lipolytica.";
RL Yeast 12:1459-1469(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes the aldol-type condensation of 2-oxoglutarate with
CC acetyl-CoA to yield homocitrate. Carries out the first step of the
CC alpha-aminoadipate (AAA) lysine biosynthesis pathway.
CC {ECO:0000250|UniProtKB:O87198}.
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:0000250|UniProtKB:O87198};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC {ECO:0000250|UniProtKB:O87198}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. Homocitrate synthase LYS20/LYS21 subfamily. {ECO:0000305}.
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DR EMBL; Z49114; CAA88928.1; -; Genomic_DNA.
DR EMBL; CR382132; CAG78892.1; -; Genomic_DNA.
DR RefSeq; XP_506079.1; XM_506079.1.
DR AlphaFoldDB; Q12726; -.
DR SMR; Q12726; -.
DR STRING; 4952.CAG78892; -.
DR EnsemblFungi; CAG78892; CAG78892; YALI0_F31075g.
DR GeneID; 2907696; -.
DR KEGG; yli:YALI0F31075g; -.
DR VEuPathDB; FungiDB:YALI0_F31075g; -.
DR HOGENOM; CLU_022158_2_2_1; -.
DR InParanoid; Q12726; -.
DR OMA; NTMRMLV; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004410; F:homocitrate synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02222; Homocitr_synth_fung_arch; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011872; Homocitrate_synth_fun/arc.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR02146; LysS_fung_arch; 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 Amino-acid biosynthesis; Lysine biosynthesis; Magnesium; Manganese;
KW Metal-binding; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..446
FT /note="Homocitrate synthase, mitochondrial"
FT /id="PRO_0000001050"
FT DOMAIN 48..307
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 56
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 116
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 176
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 210
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
SQ SEQUENCE 446 AA; 48437 MW; 90986D83D8A85250 CRC64;
MCATDNAPAA NAAPEKPSNV GVEVGHTGEQ TNPYGANPAD FLSNVSKFQL IESTLREGEQ
FASAFFDTET KIEIAKALDD FGVDYIELTS PAASEQSRSD CEAICKLGLK AKILTHIRCH
MDDARLAVST GVDGVDVVIG TSQFLRQYSH GKDMNYIAQS AVEVIEFVKS HGIEIRFSSE
DSFRSDLVDL LNIYRTVDKI GVNRVGIADT VGCANPRQVY ELVRTLKSVV SCDIECHFHN
DTGCAIANAY TALEAGANLI DVSVLGIGER NGITSLGGLM ARMIAADRDY VLSKYKLHKL
RDLENLVADA VQVNIPFNNP ITGFCAFTHK AGIHAKAILA NPSTYEILNP ADFGLTRYIH
FANRLTGWNA IKSRVDQLNL HLTDAQCKDV TAKIKKLGDV RSLNIDDVDS IIREFHADVT
STPTVAATEG PAVEDEPAAK KAKTEE
