ID G4RMH4_THETK Unreviewed; 478 AA.
AC G4RMH4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Homocitrate synthase {ECO:0000256|ARBA:ARBA00012974, ECO:0000256|HAMAP-Rule:MF_02222};
DE Short=HCS {ECO:0000256|HAMAP-Rule:MF_02222};
DE EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974, ECO:0000256|HAMAP-Rule:MF_02222};
GN Name=leuA-1 {ECO:0000313|EMBL:CCC80805.1};
GN OrderedLocusNames=TTX_0128 {ECO:0000313|EMBL:CCC80805.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC80805.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC80805.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
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:0000256|HAMAP-Rule:MF_02222}.
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|HAMAP-Rule:MF_02222};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02222};
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, ECO:0000256|HAMAP-Rule:MF_02222}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. Homocitrate synthase LYS20/LYS21 subfamily.
CC {ECO:0000256|ARBA:ARBA00006361, ECO:0000256|HAMAP-Rule:MF_02222}.
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DR EMBL; FN869859; CCC80805.1; -; Genomic_DNA.
DR RefSeq; WP_014126063.1; NC_016070.1.
DR AlphaFoldDB; G4RMH4; -.
DR STRING; 768679.TTX_0128; -.
DR PaxDb; 768679-TTX_0128; -.
DR GeneID; 11263137; -.
DR KEGG; ttn:TTX_0128; -.
DR PATRIC; fig|768679.9.peg.133; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_4_0_2; -.
DR OrthoDB; 6555at2157; -.
DR UniPathway; UPA00033; UER00028.
DR Proteomes; UP000002654; 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 CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.70.920; -; 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; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR011872; Homocitrate_synth.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR NCBIfam; TIGR02146; LysS_fung_arch; 1.
DR PANTHER; PTHR10277:SF63; HOMOCITRATE SYNTHASE; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:CCC80805.1};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02222};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_02222}; Magnesium {ECO:0000256|HAMAP-Rule:MF_02222};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_02222};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02222};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02222, ECO:0000313|EMBL:CCC80805.1}.
FT DOMAIN 13..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT ACT_SITE 301
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 21
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 85
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 145
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 179
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02222"
SQ SEQUENCE 478 AA; 52274 MW; 23A4053AD945A6BF CRC64;
MGRFSRHEFG ESIKILDSTL REGEQTPGVI FSEEWRIKIA KSLSDVGVHL IEVGDPNVAP
DVRSAISKII ALKRDGEIKS EIVVHSRSVK SDIENATSLE PDRVAIFYGV SDIHLKHKHR
KTREEALAII AEHVEFARGA GVKVRFTAED ATRADLDYLI QVVKTARDAG ADRVSIADTV
GILTPDRARQ LFSKLKEAVP GVGLDIHAHN DLGMAVANSM AATEGGADVV HTTVNGLGER
AGITPLQVFV AAYYYHKGVK LIDMAKLPYL ASLVEAASGI AQMPTFPITG DNVFTHKAGV
HQAGVLANPE TYEPFPPEVV GRSRDFSLDK YSGRRAVAHR LERLGVKVDE ETLAKVVEEL
KSTNARRLRD EDLLEILEKV TGVRYKAYVN KHIEAFIWIK VDENVYTTSV ARRVSTISGV
VNVGEVTGDF DIVARVVASN AEELNRIIED IRSVRGVKST LTNIVLKQLG SLQAPSAP
//
