ID S3DKP5_GLAL2 Unreviewed; 493 AA.
AC S3DKP5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN ORFNames=GLAREA_07760 {ECO:0000313|EMBL:EPE32626.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE32626.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE32626.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(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; KE145359; EPE32626.1; -; Genomic_DNA.
DR RefSeq; XP_008080638.1; XM_008082447.1.
DR AlphaFoldDB; S3DKP5; -.
DR STRING; 1116229.S3DKP5; -.
DR GeneID; 19466812; -.
DR KEGG; glz:GLAREA_07760; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_022158_2_2_1; -.
DR OMA; NTMRMLV; -.
DR OrthoDB; 2781767at2759; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000016922; 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:UP000016922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 68..321
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 13..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 53759 MW; 8EC091E02B488CE5 CRC64;
MCPSCEPEAI ANGNGHTNGQ SNGNGASNGN GNSSSHPGYT GIETKANPHH RSNPYQPVGD
FLSNVNNFKI IESTLREGEQ FANAFFDTEK KIEIAKALDD FGVDYIELTS PAASEQSRLD
CEAICKLGLK AKILTHIRCH MDDARIAVQT GVDGVDVVIG TSSYLMEHSH GKDMTYITNT
AIEVINYVKS HNIEIRFSSE DSFRSNLVDL LSIYSTVDKI GVNRVGIADT VGCASPRQVY
DLIRTLRGVV SCDIETHFHN DTGCAIANAY CALEAGATHI DTSVLGIGER NGITPLGGLM
ARMIVADREY VMGKYKLDKL KDIEDLVAQA VEVNIPFNNP ITGFCAFTHK AGIHAKAILN
NPSTYEIINP ADFGMTRYVH FASRLTGWNA IKSRAVQLKI DMTDAQYKEC TTKIKALADI
RPIAVDDADS IIRAFHRGLK LGKPVDLLPN MTDAERAALA EKEKEIDIPE KRSLDEEANT
PVPSKKNKNG ITA
//
