ID   A0A1G8UT84_9EURY        Unreviewed;       345 AA.
AC   A0A1G8UT84;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=2-isopropylmalate synthase {ECO:0000313|EMBL:SDJ56874.1};
GN   ORFNames=SAMN05216226_105100 {ECO:0000313|EMBL:SDJ56874.1};
OS   Halovenus aranensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halovenus.
OX   NCBI_TaxID=890420 {ECO:0000313|EMBL:SDJ56874.1, ECO:0000313|Proteomes:UP000198856};
RN   [1] {ECO:0000313|EMBL:SDJ56874.1, ECO:0000313|Proteomes:UP000198856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M10015 {ECO:0000313|EMBL:SDJ56874.1,
RC   ECO:0000313|Proteomes:UP000198856};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|ARBA:ARBA00006154}.
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DR   EMBL; FNFC01000005; SDJ56874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8UT84; -.
DR   STRING; 890420.SAMN05216226_105100; -.
DR   Proteomes; UP000198856; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR   PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198856};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..219
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   345 AA;  36592 MW;  3AB9CF5410F5B6B6 CRC64;
     MGTHVIEAGF PVNSDDEFEA VRDIAAASSS TVCGLARVVD DDIEAALDSG VDMVHVFAST
     SDVQLEDSMH ATRTEAKQRA VQSVRRVVEA GATCMFSPMD ATRTDEAFLF EMVEAAADAG
     TDWINVPDTC GVATPERFGE LVADIVEHSG DARVDVHTHD DFGLATPNAL AGVRGGADQV
     QVSVNGIGER AGNAAYEEVV MGLESLYDVD TGIDTTGIAD ISRTVEQRSA VPVPGNKPVV
     GDNAFAHESG IHAAGVIENS ETFEPGVMTP EMVGAEREFV LGKHTGTHSV RKRLEEVGFD
     PTDEEVHTVT QKVKESGVSA GHVTATDLEQ FARDAGIARR EEVRV
//