ID A0A2K5ARX9_9ARCH Unreviewed; 526 AA.
AC A0A2K5ARX9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00030312};
GN Name=leuA {ECO:0000313|EMBL:SPC34401.1};
GN ORFNames=NCAV_1234 {ECO:0000313|EMBL:SPC34401.1};
OS Candidatus Nitrosocaldus cavascurensis.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Candidatus Nitrosocaldales;
OC Candidatus Nitrosocaldaceae; Candidatus Nitrosocaldus.
OX NCBI_TaxID=2058097 {ECO:0000313|EMBL:SPC34401.1, ECO:0000313|Proteomes:UP000236248};
RN [1] {ECO:0000313|Proteomes:UP000236248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCU2 {ECO:0000313|Proteomes:UP000236248};
RA Kerou L M.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000064};
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|ARBA:ARBA00006154, ECO:0000256|RuleBase:RU003523}.
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DR EMBL; LT981265; SPC34401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K5ARX9; -.
DR KEGG; ncv:NCAV_1234; -.
DR Proteomes; UP000236248; Chromosome ncav.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
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; IPR011830; LEU1_arch.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR02090; LEU1_arch; 1.
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:SPC34401.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 21..272
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 526 AA; 57212 MW; CAE177D74D55438A CRC64;
MSSDVSNSIS NSDSSNSVDY VRIYDTTLRD GEQTPGVTLT PEDKLLIAIQ LDKLGVDVIE
AGFPIVSQGE KEAVKMIVKQ GLNSEISVLA RTDKRDIDAA IDCGVRYVHT FIATSDIHLQ
YKLKISREEA IRKAVDAIEY CKAHGLYVEF SAEDATRSDR EYLKQVYKAV VDAGADRIDV
PDTVGYATPK YIHSLITELR STVKVPISIH CHDDFGLAVA NSIAAIEAGA ECAHVTINGL
GERAGNASLE EFVMALHCLY NKRTRINTKL LYETSKLVAS LTGIIVQPNK AIVGENAFGH
ESGIHTHGVL SNPLCYEPIS PELVGRKRWL EAGKHAGMHG IAAMLAEYGI RPEQEQLRQI
VAKVKELGDK GKQVTDADLI AIASQVMNQQ NLVEHVRLMD FVVTTGINVV PTASVRLIID
GKEYIVAETG VGPVDAALKA IQKITDRIAS IRLSEFRLEA ISGGSDALAE VSVKVEDSNG
KISSARATGE DIVVASVQAM INGINKMMMK RTIDRDSNRE IQGYTV
//