ID A2SR21_METLZ Unreviewed; 522 AA.
AC A2SR21;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993};
GN OrderedLocusNames=Mlab_0603 {ECO:0000313|EMBL:ABN06777.1};
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358 {ECO:0000313|EMBL:ABN06777.1, ECO:0000313|Proteomes:UP000000365};
RN [1] {ECO:0000313|EMBL:ABN06777.1, ECO:0000313|Proteomes:UP000000365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z {ECO:0000313|Proteomes:UP000000365};
RX PubMed=21304657; DOI=10.4056.sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate).
CC {ECO:0000256|ARBA:ARBA00003715}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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DR EMBL; CP000559; ABN06777.1; -; Genomic_DNA.
DR AlphaFoldDB; A2SR21; -.
DR STRING; 410358.Mlab_0603; -.
DR KEGG; mla:Mlab_0603; -.
DR eggNOG; arCOG02092; Archaea.
DR HOGENOM; CLU_022158_0_1_2; -.
DR OrthoDB; 6555at2157; -.
DR Proteomes; UP000000365; Chromosome.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 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 Acyltransferase {ECO:0000313|EMBL:ABN06777.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Reference proteome {ECO:0000313|Proteomes:UP000000365};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 27..279
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 522 AA; 56587 MW; D7BAE7B840936DCB CRC64;
MGSEQSLRKW RIAFYCDKST VNTNRRVTIL DTTLRDGEQT PGVSFTLEQK IEIAHQLSDI
GVDVIEAGFP ASSDVEFETV KRICAEEGIR PKICGLARSV KADVDRCIEA GVDMVHVFIP
TSEIQRTYTI KKSHAEVLAI TREIITYARS KCDYVMFSPM DATRTEPSEL IEICKAADEA
GTTIINIPDT VGVSTPSMIK PLIAMIRENV KCKIDVHCHN DFGLATANTI AAVEGGADQI
QVTVNGIGER AGNADLAQTV MILKSIYGIE TNIRTEKLVE TSRMVSRFSQ IAVLPIQPVV
GENAFSHESG IHSHGVMANP GTFEPGIMTP EMVGHRRRLK LGKHVGKHAV RQMLEDINVN
PSDPELDMIV AKVKEISGRG RKVTEFDLFE IAKIITGSHN DKKMIELDDI SVFTGSHAIP
TASVQAVVHG ENKICSKTGD GPVDAAMKAL LAIAPGKVQL KSFQIEAISG GSDALGCVTI
EVEDEKGRIF DAASSNSDIV IASAEAMVNA LNVVYRSGGF DR
//
