HOSA_SACS2
ID HOSA_SACS2 Reviewed; 461 AA.
AC Q97ZE0;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SSO0977;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; AE006641; AAK41252.1; -; Genomic_DNA.
DR PIR; E90249; E90249.
DR RefSeq; WP_009992429.1; NC_002754.1.
DR AlphaFoldDB; Q97ZE0; -.
DR SMR; Q97ZE0; -.
DR STRING; 273057.SSO0977; -.
DR EnsemblBacteria; AAK41252; AAK41252; SSO0977.
DR GeneID; 44129910; -.
DR KEGG; sso:SSO0977; -.
DR PATRIC; fig|273057.12.peg.977; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_4_0_2; -.
DR InParanoid; Q97ZE0; -.
DR OMA; DWSNGMR; -.
DR PhylomeDB; Q97ZE0; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IBA:GO_Central.
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:0009098; P:leucine biosynthetic process; IBA:GO_Central.
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; 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; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Lysine biosynthesis; Magnesium; Manganese;
KW Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..461
FT /note="Homocitrate synthase"
FT /id="PRO_0000140423"
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; 50882 MW; E87E9E4CA21BA56F CRC64;
MIKVGILDST LREGEQTPGV IFTVDQRVEI AKALSDLGVS MIEAGHPAVS PDIYEGIKRI
VKLKKEGIIT SEIVGHSRAV KRDIEIAAEL EVDRIAIFYG VSDIHLKAKH KATREEALRV
IAETISYARS HGVKVRFTAE DGSRTDFDFL VTVSRTARDA GADRVSIADT VGILYPSKTK
ELFSALIREV PNLEYDIHAH NDLGLAVANA LAAVEGGATI VHATVNGLGE RVGIVPLQQI
VAAIKYHFGI EVVKLDKLQY VSSLIEKYSG IPMPPNYPIT GDYAFLHKAG VHVAGVLSDP
RTYEFMPPET FGRTRDYTID KYTGKHALRD KYEKLGVKIS EAEMDQILAK IKSNTTIRFY
RDVDLLELAE EVTGRVLKPR PPEQIEALIS VKCDSNVYTT SVTRRLSVIN GVKEVMEISG
DYDILVKVQA KDSNELNQII ESIRATKGVR STLTSLVLKK M
