HOSA_SULIK
ID HOSA_SULIK Reviewed; 461 AA.
AC C4KGW9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Homocitrate synthase {ECO:0000255|HAMAP-Rule:MF_02222};
DE Short=HCS {ECO:0000255|HAMAP-Rule:MF_02222};
DE EC=2.3.3.14 {ECO:0000250|UniProtKB:O87198, ECO:0000255|HAMAP-Rule:MF_02222};
GN OrderedLocusNames=M164_1229;
OS Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=426118;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.4 / Kamchatka #3;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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 -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. Homocitrate synthase LYS20/LYS21 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02222}.
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DR EMBL; CP001402; ACR41833.1; -; Genomic_DNA.
DR RefSeq; WP_012711253.1; NC_012726.1.
DR AlphaFoldDB; C4KGW9; -.
DR SMR; C4KGW9; -.
DR EnsemblBacteria; ACR41833; ACR41833; M164_1229.
DR GeneID; 7814454; -.
DR GeneID; 7940569; -.
DR KEGG; sid:M164_1229; -.
DR HOGENOM; CLU_022158_4_0_2; -.
DR OMA; DWSNGMR; -.
DR BioCyc; SISL426118:GI01-1257-MON; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000001479; Chromosome.
DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
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; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR011872; Homocitrate_synth_fun/arc.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR02146; LysS_fung_arch; 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; Transferase.
FT CHAIN 1..461
FT /note="Homocitrate synthase"
FT /id="PRO_1000213318"
FT DOMAIN 4..259
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 12
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 76
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 136
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 170
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
SQ SEQUENCE 461 AA; 50825 MW; 1067BD15BAEF4646 CRC64;
MIKVGILDST LREGEQTPGV IFTVDQRVEI AKALSDLGVS MIEAGHPAVS PDIYEGIKRI
VKLKKEGIIT SEIVGHSRAV KRDIEIAAEL EVDRIAIFYG VSDLHLKAKH KATREEALRT
IAETISYAKN HGVKVRFTAE DGSRTDFDFL VTVSKTARDA GADRVSIADT VGILYPSKTK
ELFSALTREV PNLEFDIHAH NDLGLAVANA LAAIEGGATI IHATVNGLGE RVGIVPLQQI
AAAIKYHFGI EVVKLDKLQY VSSLVEKYSG IPMPPNYPIT GDYAFLHKAG VHVAGVLNDP
RTYEFMPPET FGRTRDYTID KYTGKHALRD KYEKLGVKIS DAEMDQILAK IKSNTTIRFY
RDVDLLELAE EVTGRVLKPR PPEQIEALIS VKCDSNVYTT SVTRRLSVIN GVKEVMEISG
DYDILVKVQA KDSNELNQII ESIRATKGVR STLTSLVLKK M
